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Database: UniProt
Entry: Q18AS5_PEPD6
LinkDB: Q18AS5_PEPD6
Original site: Q18AS5_PEPD6 
ID   Q18AS5_PEPD6            Unreviewed;       464 AA.
AC   Q18AS5;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=CD630_10720 {ECO:0000313|EMBL:CAJ67916.1};
OS   Peptoclostridium difficile (strain 630) (Clostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Clostridioides.
OX   NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67916.1, ECO:0000313|Proteomes:UP000001978};
RN   [1] {ECO:0000313|EMBL:CAJ67916.1, ECO:0000313|Proteomes:UP000001978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630 {ECO:0000313|EMBL:CAJ67916.1,
RC   ECO:0000313|Proteomes:UP000001978};
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ67916.1; -; Genomic_DNA.
DR   RefSeq; WP_011861085.1; NC_009089.1.
DR   RefSeq; YP_001087556.1; NC_009089.1.
DR   ProteinModelPortal; Q18AS5; -.
DR   STRING; 272563.CD1072; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; CAJ67916; CAJ67916; CD630_10720.
DR   GeneID; 31352641; -.
DR   GeneID; 4915674; -.
DR   KEGG; cdf:CD630_10720; -.
DR   KEGG; pdc:CDIF630_01216; -.
DR   PATRIC; fig|272563.120.peg.1115; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   BioCyc; PDIF272563:G12WB-1195-MONOMER; -.
DR   Proteomes; UP000001978; 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:CAJ67916.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001978};
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:UP000001978};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   464 AA;  51387 MW;  92856FE89D48C3CB CRC64;
     MNLKYEFKNA WDFERKENTI EQIMQYSSNY MEFLSKSKTE RLSVKEIIKL AKENNYISID
     EAMEKGSISC GDKIYVINKE KAVALFVIGK NYIEKGMKII GSHIDSPRLD LKPNPLYQES
     NLGFFKTHYY GGIKKYQWTA IPLALHGIVI LNDGTKVDIS IGEEDSDPVF CVTDLLIHLA
     GDQMQKKLSE GISGEALNIL IGNIPLEDEE KEPITANILK ILNEKYNIVE EDLLSAEIEV
     VPAGKARDLG LDRSMVLGYG HDDRVCSYAA VKAILETEQP EFTSVALCVD KEEIGSKGNT
     GMHSKFFENT VAELIALEGD YCDIKVRRAL ANSKVLSADV SAGYDPNFGE AYEKRNSAYM
     GNGVVLTKYT GSRGKSGCND ANAEFMSEVK GIFNKGNVIW QTAELGKVDQ GGGGTIAHIL
     ANQGAEVIDC GVGVLNMHAP HEIVSKVDIY EMYKGYKAFF NINL
//
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