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Database: UniProt
Entry: B5Y7J5_COPPD
LinkDB: B5Y7J5_COPPD
Original site: B5Y7J5_COPPD 
ID   B5Y7J5_COPPD            Unreviewed;       461 AA.
AC   B5Y7J5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   22-NOV-2017, entry version 53.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=lap {ECO:0000313|EMBL:ACI16793.1};
GN   OrderedLocusNames=COPRO5265_0376 {ECO:0000313|EMBL:ACI16793.1};
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermodesulfobiaceae; Coprothermobacter.
OX   NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI16793.1, ECO:0000313|Proteomes:UP000001732};
RN   [1] {ECO:0000313|Proteomes:UP000001732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / BT {ECO:0000313|Proteomes:UP000001732};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus
RT   strain ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) 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; CP001145; ACI16793.1; -; Genomic_DNA.
DR   RefSeq; WP_012543445.1; NC_011295.1.
DR   ProteinModelPortal; B5Y7J5; -.
DR   STRING; 309798.COPRO5265_0376; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ACI16793; ACI16793; COPRO5265_0376.
DR   KEGG; cpo:COPRO5265_0376; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000001732; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACI16793.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001732};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACI16793.1};
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:UP000001732};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   461 AA;  51025 MW;  E0377A1E65AC03A2 CRC64;
     MINWKNGHLK VDETTLSEIE SFAKDYMQFM AVAKTERETV TQSIKEAREK GFRNLDELEG
     SWRPGEKVYF ENRKKSVVFA VLGQKPATEG VNIVVAHVDA PRLDLKPRPL KEDEQIAILE
     THYYGGIKNF HWVSTPLALH GVVVKTDGTV VEIAVGDKDE DPVLVIPDIL PHLGRKIQMS
     KTMDEAIPGE SLDVVIGSVP LKDEEKEPVK KFILKLLNDT YGITEADFLS AELEVVPALK
     PREVGLDRAL IGAYAQDDRV CGYTAFRALL DLAEVPEKTA VVILADKEEV GSMGNTGMRS
     AFIDKFLSKL IALTKPSFSP LDLYEAWNRT KVLSADVTAA VDPIWKSVHE MQNAARMHYG
     PVLTKYTGSR GKGGANDAHA EFLAQVREAF DKEGVIWQMA ELGKVDEGGG GTVALFMADR
     GADVVDIGVA LWGMHSLFEV SSKLDVYYAY KANQAFFKHL K
//
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