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Database: UniProt
Entry: F7V8W1_CLOSS
LinkDB: F7V8W1_CLOSS
Original site: F7V8W1_CLOSS 
ID   F7V8W1_CLOSS            Unreviewed;       429 AA.
AC   F7V8W1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=CXIVA_06040 {ECO:0000313|EMBL:BAK46571.1};
OS   Clostridium sp. (strain SY8519).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK46571.1, ECO:0000313|Proteomes:UP000008937};
RN   [1] {ECO:0000313|Proteomes:UP000008937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX   PubMed=21914882; DOI=10.1128/JB.05637-11;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genomic sequence of the O-desmethylangolensin-producing
RT   bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from
RT   adult human intestine.";
RL   J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK46571.1; -; Genomic_DNA.
DR   RefSeq; WP_013976555.1; NC_015737.1.
DR   STRING; 1042156.CXIVA_06040; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; BAK46571; BAK46571; CXIVA_06040.
DR   KEGG; cls:CXIVA_06040; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000008937; 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   Complete proteome {ECO:0000313|Proteomes:UP000008937};
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:UP000008937};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   429 AA;  47774 MW;  02416992235D6EBB CRC64;
     MEERQTAEAL MEAIRKSPSC FHVIRNMEQR FREAGFEKLR EDRDWNLARG KNYYVTRNAS
     SILAFRIPER PFSAMHLMAS HSDSPTFKIK PAPEVNGGSC VRLNMEKYGG MILHTWLDRP
     LSVAGRLLCE TEEGICQRLV APDKDLLIIP SLAIHMDRTA NSGLTLNPQE DMLPVFSLEG
     SSTSFFQLMA EEAGVAEEQI LGTDLFLVNR QQPAWIGAEQ EFLAAPKLDD LECAYLTQWG
     FLESRSENLT VHAVFDNEEV GSTTRQGAAS TFLADTLQRI AEGLGMSGSD YRRILAGSFM
     ISADNAHAAH PGHLGKADPT NRPVINGGIV LKYHANQKYT TDGVSEAYFK TVCRKAGVPW
     QTFANRSDMN GGSTLGNISN TQVSVRTADI GLPQWAMHSS YETGGSRDPK YLLDFSRTFY
     EMEPCRIKE
//
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