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Database: UniProt
Entry: C6PVQ2_9CLOT
LinkDB: C6PVQ2_9CLOT
Original site: C6PVQ2_9CLOT 
ID   C6PVQ2_9CLOT            Unreviewed;       477 AA.
AC   C6PVQ2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 35.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CcarbDRAFT_2869 {ECO:0000313|EMBL:EET86676.1};
OS   Clostridium carboxidivorans P7.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86676.1, ECO:0000313|Proteomes:UP000004198};
RN   [1] {ECO:0000313|EMBL:EET86676.1, ECO:0000313|Proteomes:UP000004198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7 {ECO:0000313|EMBL:EET86676.1,
RC   ECO:0000313|Proteomes:UP000004198};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Hemme C.L.;
RT   "The draft genome of Clostridium carboxidivorans P7.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EET86676.1}.
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DR   EMBL; ACVI01000047; EET86676.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6PVQ2; -.
DR   STRING; 536227.CcarbDRAFT_2869; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EET86676; EET86676; CcarbDRAFT_2869.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   Proteomes; UP000004198; Unassembled WGS sequence.
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:EET86676.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004198};
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:UP000004198};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   477 AA;  53759 MW;  92AFEEE18454E174 CRC64;
     MNARYREGIL VMNEDLTKKY EYAWDKYSKD DLKDVFHLSD KYKTFMSKCK TERECVEEFI
     IRAEEAGFKN LEDVVSKNGT LKSGDKIYAN NKGKGLALFV IGNKKFEDGM RILGAHVDSP
     RLDLKQNPLY EDTDMALFET HYYGGIKKYQ WVTLPLAIHG VIIKKDGTKV NVAIGEDDND
     PVLGVSDLLV HLASEQMEKK ANKVIEGEDL NVLVGSMPIE DKEAKDRVKR NILNILNEKY
     SIVEEDFVSA ELEIVPAGKA RDYGLDRSMI MAYGHDDRIC SYTSFEAMLK LEKSDKTCVA
     LFVDKEEIGS VGSTGMHSRF FENTVAEVMN LCGDYTELKL RRSLTNSKML SSDVCAAFDP
     NYPSTMEKKN CAYFGKGIVF NKYTGARGKS GCNDANPEYI AQIRAIMEKH NVSWQTSELG
     KVDQGGGGTI AYILAQYNME VIDCGVALHN MHSPWEIASK ADIYETMRAY YSFLLEA
//
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