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Database: UniProt
Entry: G8LU53_CLOCD
LinkDB: G8LU53_CLOCD
Original site: G8LU53_CLOCD 
ID   G8LU53_CLOCD            Unreviewed;       484 AA.
AC   G8LU53;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   07-JUN-2017, entry version 31.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Clocl_1832 {ECO:0000313|EMBL:AEV68441.1};
OS   Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=720554 {ECO:0000313|EMBL:AEV68441.1, ECO:0000313|Proteomes:UP000005435};
RN   [1] {ECO:0000313|Proteomes:UP000005435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19732 / NBRC 101661 / EBR45
RC   {ECO:0000313|Proteomes:UP000005435};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L.,
RA   Izquierdo J., Woyke T.;
RT   "Complete sequence of Clostridium clariflavum DSM 19732.";
RL   Submitted (DEC-2011) 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; CP003065; AEV68441.1; -; Genomic_DNA.
DR   RefSeq; WP_014255026.1; NC_016627.1.
DR   STRING; 720554.Clocl_1832; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AEV68441; AEV68441; Clocl_1832.
DR   KEGG; ccl:Clocl_1832; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000005435; 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:AEV68441.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005435};
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:UP000005435};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   484 AA;  53846 MW;  8D2F47002E9D28CB CRC64;
     MADNKTQGQI LSEKLLIESK SAWEKISDEE FRLTFDLCER YKTFLNKAKT EREFVEETEK
     LAKSKGYIAI EELINSQKKL MPGMKVYSIG RNKTVVLAVI GEESLEKGVN IVGAHIDSPR
     IDLKPNPVYE ANDMVFLKTH YYGGIKKYQW VTIPLAMHGV VVKRDGSKVN IKIGEDDNDT
     VFTITDLLPH LAADQMQKKM SEGITGEGLN ILSGSIPYKD DKVKDKVKLN ILNILNEKYG
     IVEEDLISAE LEMVPKFNAV DVGFDKSMIG AYGQDDRVCA YTALEAILDT EKVKRTAVCI
     LTDKEEIGSM GNTGAQSSFF VNFLADLCSL SVDNYNDIML RRCLSNSKML SADVNAAIDP
     TYENVYEKRN SSFLGRGIVL QKYTGARGKS GASDANAEFV GEIRKLFNDN NVVWQSAELG
     KVDQGGGGTI AQFIANLNVD VIDCGVAVLS MHSPFEVTSK VDVYMAYKAY KTFYINLVKE
     INFD
//
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