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Database: UniProt
Entry: A0A0A2TK30_9FIRM
LinkDB: A0A0A2TK30_9FIRM
Original site: A0A0A2TK30_9FIRM 
ID   A0A0A2TK30_9FIRM        Unreviewed;       458 AA.
AC   A0A0A2TK30;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=JT05_05175 {ECO:0000313|EMBL:KGP76397.1};
OS   Desulfosporosinus sp. Tol-M.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP76397.1, ECO:0000313|Proteomes:UP000030439};
RN   [1] {ECO:0000313|EMBL:KGP76397.1, ECO:0000313|Proteomes:UP000030439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Abu Laban N., Tan B., Dao A., Foght J.;
RT   "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable
RT   isotope probing of toluene- degrading methanogenic culture enriched
RT   from oil sands tailing of Alberta, Canada.";
RL   Submitted (OCT-2014) 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:KGP76397.1}.
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DR   EMBL; JQID01000071; KGP76397.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGP76397; KGP76397; JT05_05175.
DR   Proteomes; UP000030439; 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:KGP76397.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030439};
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:UP000030439};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   458 AA;  50890 MW;  D1DF0FBA3787D518 CRC64;
     MSSKKVKLAW DELVMSEKER QAMTEYLAFL SEGKTERKSW QLLERWAQKA DFVALDGVKG
     FKPGQKVRLA VRGKAGIIAI SGTRPLNEGF RLIAAHLDAP RLDIKQRPLY EEEGLAFLKT
     HYYGGIKKYQ WTALPLALHG VVILRDGHKV EIVVGEADED PVFTITDLLP HLAKDQYDKK
     LPEAITGEGL NLLLGHDPCN EDGEERVKLA ILHFLKDKYG IEEDDFVSAE LEVVPAGRAR
     YAGLDRSFIV GYGQDDRVCS FAAWKAIEEI EQPEWTTIVL FADKEEIGSD SNTGMKARYL
     ENFIAELISM QNGTYDGLMV RRALSRGKAL SADVAAGYDP NYAEVMDKRN SAFLGRGVVI
     SKYTGSRGKS GSSDANPEFI AEVRRIFDEA KVSWQTAELG KVDQGGGGTI AQYMAIYGME
     VLDCGVGILS MHAPWEISSV ADLIMMMRGY RAFLADKD
//
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