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Database: UniProt
Entry: D1PQI3_9FIRM
LinkDB: D1PQI3_9FIRM
Original site: D1PQI3_9FIRM 
ID   D1PQI3_9FIRM            Unreviewed;       432 AA.
AC   D1PQI3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, 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=SUBVAR_06652 {ECO:0000313|EMBL:EFB75041.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75041.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB75041.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75041.1,
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:EFB75041.1}.
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DR   EMBL; ACBY02000043; EFB75041.1; -; Genomic_DNA.
DR   RefSeq; WP_007048011.1; NZ_GG704770.1.
DR   ProteinModelPortal; D1PQI3; -.
DR   STRING; 411471.SUBVAR_06652; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EFB75041; EFB75041; SUBVAR_06652.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; SVAR411471-HMP:GMW7-2652-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:EFB75041.1};
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:EFB75041.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFB75041.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003438};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  46719 MW;  AA9C3C3551A3CE98 CRC64;
     MIDDLFEFLQ EGVTPYHAAA TAAAWLEAAG FTRLEEADYW NLEPGKGYYI LRNGSAVVAW
     RIPDHAIGGW RITASHSDAP GWKIKSDAVT NDGCRRLSVE GYGGMNMASW LDRPLTVAGR
     VLVRTEDGVE TRLVHFDRDL LVIPSLAIHM QRNVNKGHEY NPQIDMQPLW GPEGSRSLTD
     LLCEALGVAA EDILDRDLQL VTRQAPTQIG PDGEYFLAPR IDDLECAATT LLGFIDAAAE
     TDSACAPVWA MLDNEEVGSS SRQGAQSSFL RDVLDRILES IPHSAQMEHR ALANSFLLSA
     DNGHATHPNF PAKSDPAAPV RLGGGVLLKY NASQKYTTNA LSGGIFRAIC EKAGVKVQTF
     TNRADEAGGS TLGNLQSHSL PIPMADIGLP QLAMHSAVET AAVSDAEAMV RAVAAFYRVH
     LRALGDGVYT LE
//
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