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Database: UniProt
Entry: D1PKX1_9FIRM
LinkDB: D1PKX1_9FIRM
Original site: D1PKX1_9FIRM 
ID   D1PKX1_9FIRM            Unreviewed;       463 AA.
AC   D1PKX1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   07-JUN-2017, entry version 34.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SUBVAR_05006 {ECO:0000313|EMBL:EFB76629.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB76629.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB76629.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB76629.1,
RC   ECO:0000313|Proteomes:UP000003438};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (DEC-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:EFB76629.1}.
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DR   EMBL; ACBY02000020; EFB76629.1; -; Genomic_DNA.
DR   RefSeq; WP_007046409.1; NZ_GG704769.1.
DR   ProteinModelPortal; D1PKX1; -.
DR   STRING; 411471.SUBVAR_05006; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EFB76629; EFB76629; SUBVAR_05006.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; SVAR411471-HMP:GMW7-1007-MONOMER; -.
DR   Proteomes; UP000003438; 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:EFB76629.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003438};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFB76629.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFB76629.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003438};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   463 AA;  50593 MW;  A2777CCAE6A2A4ED CRC64;
     MQTTEELKKL LYKNETVADM APDVLQAAQD FCEGYKTFLD NGKTEREATA YSEKLLMEAG
     YKPFVPGQKL EAGAKVYTIN RSKCVLAATI GTKPLNEGFH LNIAHIDSPR LDLRPVPVFE
     KNGLGYLRTH YYGGVRKYQW PTMPLALHGV IYRADGSKVE ICIGEKEDDP VFCITDLLPH
     LSAKQNAKPL SEGISAEDLN VLIASQPIAD KEAEQRVKLN VLGMLHEAFG ITERDFTRAE
     IEVVPAHKAR DIGLDRAMIG AYGHDDRVDA YPALMAEIGV EKPAYTTVCV LTDKEETGSD
     GVTGLHSMYT FHFLQQLCET QEADYITACK AGKCLSADVT AAFDPTFADA FEPDNATYAG
     NGVAIYKYTG SRGKSGTSDA SAELVSYLTG LLDRNSVVWQ IGEMGKLDLG GGGTVAKFVA
     NQDIDTIDIG VPVLSMHSPF EVVSKADVYM AYLTFKAFCE DAE
//
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