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Database: UniProt
Entry: E0RVS1_BUTPB
LinkDB: E0RVS1_BUTPB
Original site: E0RVS1_BUTPB 
ID   E0RVS1_BUTPB            Unreviewed;       440 AA.
AC   E0RVS1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=bpr_I2496 {ECO:0000313|EMBL:ADL35229.1};
OS   Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS   (Clostridium proteoclasticum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL35229.1, ECO:0000313|Proteomes:UP000001299};
RN   [1] {ECO:0000313|EMBL:ADL35229.1, ECO:0000313|Proteomes:UP000001299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51982 / DSM 14932 / B316
RC   {ECO:0000313|Proteomes:UP000001299};
RX   PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA   Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C.,
RA   Kong Z., Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L.,
RA   Attwood G.T.;
RT   "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus
RT   B316(T) highlights adaptation to a polysaccharide-rich environment.";
RL   PLoS ONE 5:E11942-E11942(2010).
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; CP001810; ADL35229.1; -; Genomic_DNA.
DR   RefSeq; WP_013281882.1; NC_014387.1.
DR   ProteinModelPortal; E0RVS1; -.
DR   STRING; 515622.bpr_I2496; -.
DR   MEROPS; M18.002; -.
DR   PRIDE; E0RVS1; -.
DR   EnsemblBacteria; ADL35229; ADL35229; bpr_I2496.
DR   GeneID; 31783620; -.
DR   KEGG; bpb:bpr_I2496; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000001299; Chromosome 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000001299};
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:UP000001299};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   440 AA;  48716 MW;  7C146680039D6C7B CRC64;
     MAKKTSSKVN NTYKDITARM LNFIDESPTC FQVIDNLKKR LVAEGYEELD EAKEWKIAPA
     GKGKGGKYFV TRNDSSIISF RVPKKDFKGF YMIASHSDSP SFKIKENPEM EVPGAYIKLN
     VEKYGGMLCA EWFDRPLSVA GRLIVKGKNG KAETKLVNVD KDLLMLPALA IHMNREANDG
     YKYNAQKDML PIFGDDSAKD KFFDVVAKAA GVKKDDIYSH DLFLYNRVKP TVWGASDEYI
     ASSRLDDQEC VYTTFEGFLN AADSENVAVH CVFDNEEVGS GTKQGAASTF LKDTLTRINE
     CLGRTNEQYY TAVAQSFMIS ADNAHAIHPN NLDKADPVNR PVMNKGIVIK YNANQRYTTD
     AVSAATFKIM CEKAGVPYQS FTNRSDMPGG STLGNISTTQ VAVNTVDIGL AQLAMHSPYE
     TAGSKDPEYL AAVSQVFYES
//
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