(data stored in SCRATCH zone)

SWISSPROT: Q500Q3_PSEU2

ID   Q500Q3_PSEU2            Unreviewed;       683 AA.
AC   Q500Q3;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   SubName: Full=Oligopeptidase A, Metallo peptidase, MEROPS family M03A {ECO:0000313|EMBL:AAY35119.1};
DE            EC=3.4.24.70 {ECO:0000313|EMBL:AAY35119.1};
GN   OrderedLocusNames=Psyr_0045 {ECO:0000313|EMBL:AAY35119.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35119.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35119.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35119.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP000075; AAY35119.1; -; Genomic_DNA.
DR   RefSeq; WP_011266147.1; NC_007005.1.
DR   RefSeq; YP_233157.1; NC_007005.1.
DR   STRING; 205918.Psyr_0045; -.
DR   MEROPS; M03.004; -.
DR   EnsemblBacteria; AAY35119; AAY35119; Psyr_0045.
DR   GeneID; 3365520; -.
DR   KEGG; psb:Psyr_0045; -.
DR   PATRIC; fig|205918.7.peg.44; -.
DR   eggNOG; ENOG4105DGW; Bacteria.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245986; -.
DR   KO; K01414; -.
DR   OMA; KNFQSAM; -.
DR   BioCyc; PSYR205918:G1G4J-45-MONOMER; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500Q3.
DR   SWISS-2DPAGE; Q500Q3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435,
KW   ECO:0000313|EMBL:AAY35119.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      225    676       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   683 AA;  75632 MW;  B51740B2EBCA5FDB CRC64;
     MSANNPLLQS YDLPPFSAIR AEHVKPAIEQ ILADNRAAIA DILAKQGSTP TWAGLVLTMD
     ELNDRLGAAW SPVSHLNAVC NSAELREAYE SCLPALSAYS TEMGQNRALF QAYEALANGP
     EAASFDVGQK TILEQSLRDF RLSGIDLPPE QQKRYAEVQS KLSELGSQFS NQLLDATQAW
     TKLVADESAL AGLTDSAKQQ MAAAAKAKDL EGYLITLEFP NYYAVMTYAE DRALREEVYA
     AYATRASDQG PNAGKNDNTP VMEQILDLRQ ELAQLLGYAN YAELSLATKM AESSDQVLSF
     LRDLAKRSKP FAAQDLEQLK AYAAEQGCPD LQSWDSGFYG EKLREQRYSV SQEILRAYFP
     VDKVLDGLFT IVQRLYGIEI AEQKGFDTWH PDVRLFEIKE NGQHVGRFFF DLYARANKRG
     GAWMDGARDR RRTAQGTLQS PVANLVCNFT PAVAGKPALL THDEVTTLFH EFGHGLHHLL
     TRVEHAGVSG INGVAWDAVE LPSQFMENWC WEPEGLALIS GHYETGEPLP QDLLEKMLAA
     KNFQSGLMMV RQLEFSLFDF ELHATHGDGR SVLEVLEGIR DEVSVMRPPA YNRFPNSFAH
     IFAGGYAAGY YSYKWAEVLS ADAFSKFEED GVLNAETGRA FREAILARGG SQAPMVLFVD
     FRGREPSIDA LLRHSGLSED AAA
//

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