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Database: UniProt
Entry: D1BM36_VEIPT
LinkDB: D1BM36_VEIPT
Original site: D1BM36_VEIPT 
ID   D1BM36_VEIPT            Unreviewed;       463 AA.
AC   D1BM36;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Vpar_0762 {ECO:0000313|EMBL:ACZ24443.1};
OS   Veillonella parvula (strain ATCC 10790 / DSM 2008 / JCM 12972 / Te3)
OS   (Veillonella alcalescens).
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=479436 {ECO:0000313|EMBL:ACZ24443.1, ECO:0000313|Proteomes:UP000007968};
RN   [1] {ECO:0000313|Proteomes:UP000007968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3
RC   {ECO:0000313|Proteomes:UP000007968};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Wellnitz S., Schneider S., Gronow S.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete genome of Veillonella parvula DSM 2008.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP001820; ACZ24443.1; -; Genomic_DNA.
DR   RefSeq; WP_012864239.1; NC_013520.1.
DR   ProteinModelPortal; D1BM36; -.
DR   STRING; 479436.Vpar_0762; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ACZ24443; ACZ24443; Vpar_0762.
DR   GeneID; 8636223; -.
DR   KEGG; vpr:Vpar_0762; -.
DR   PATRIC; fig|479436.6.peg.741; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   BioCyc; VPAR479436:GHOS-776-MONOMER; -.
DR   Proteomes; UP000007968; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACZ24443.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007968};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007968};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   463 AA;  51456 MW;  107A8B608CB76A51 CRC64;
     MERKYAWHNY DDATMEKVYA LSDTYRQFLD NGKTERECVV QAVEFAEAKG YINLNDIIKS
     NTSIKAGDKI YYTHMDKSIA LFNIGTDDIE LGMNILGAHI DSPRIDVKQN PQYEDSNLVF
     WDTHYYGGIK KYHWVAMPLA IHGVVVKTDG TRININIGDK ETDPVFCITD LLPHLGQEQM
     QKNAAKVIEG EALDLLIGSR PVKDEEKEGV TKFINSLLEK EYGFIERDLL SAELEIVPAG
     KARDMGFDRS MVMAYGQDDR VCAYTSLVAM LEVDNVKRTT CCLLVDKEEI GSVGATGMQS
     RFFENAVAEI LTLMGKPNSV SVRRTLEKSR MLSSDVSAGY DPLYASAYEK KNASYLGMGV
     VFNKFTGSRG KAGSNDANAE YMGFIRRVME SNNVTYQTAE LGKVDLGGGG TIAYIMALYG
     MNVIDCGVAV LSMHAPWEVT SKADIYEAKQ CYVAFLNAAD ESI
//
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