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Database: UniProt
Entry: A0A101HWV4_9FIRM
LinkDB: A0A101HWV4_9FIRM
Original site: A0A101HWV4_9FIRM 
ID   A0A101HWV4_9FIRM        Unreviewed;       467 AA.
AC   A0A101HWV4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   07-JUN-2017, entry version 5.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=XE00_0448 {ECO:0000313|EMBL:KUK84921.1};
OS   Desulfotomaculum kuznetsovii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=58135 {ECO:0000313|EMBL:KUK84921.1, ECO:0000313|Proteomes:UP000054111};
RN   [1] {ECO:0000313|EMBL:KUK84921.1, ECO:0000313|Proteomes:UP000054111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=45_62 {ECO:0000313|EMBL:KUK84921.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK84921.1}.
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DR   EMBL; LGGU01000007; KUK84921.1; -; Genomic_DNA.
DR   PATRIC; fig|58135.3.peg.474; -.
DR   Proteomes; UP000054111; 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:KUK84921.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054111};
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:UP000054111};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   467 AA;  51097 MW;  884B7D1E3ED03120 CRC64;
     MEDKGQSKGE SYESKHVWDC LDDAGRQDVM EFCERYRDFL DAAKTEREAV DTIIARAEIG
     GFTPLTEQSR IVPGSRVYSA KHGKVMAMAV IGSEPLEKGL NVIGSHIDAP RLDLKPRPLY
     QEAGLALFKT HYYGGIKKYQ WVSIPLSLHG VVFTKEGNAV RIAIGSNDHD PVFTIADLLP
     HLAKDQMEKK MSEAVKGEAL NVLVGGNPVE NREVKERLKQ AVLDQLNARY GLIEEDFISA
     ELEVAPAFPA RDVGFDRSMI GGYGQDDRVC AFTSLQAILE LDSVSRTAVA LFADKEEIGS
     VGNTGMESVF LTNFIAELAG CSLPQYSELT VRRILANSRA LSADVTAGTN PSYTEVMDKH
     NEMLLGRGTA FHKYGGGGGK RSSSDANAEF VSFVRQLFNK EGVVWQTGEL GKVDQGGGGT
     IAYLLAHYGM DVLDCGVPLL GMHSPFEVAH KGDIYMTYKG YKVFFKA
//
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