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Database: UniProt
Entry: D4N133_ANAHA
LinkDB: D4N133_ANAHA
Original site: D4N133_ANAHA 
ID   D4N133_ANAHA            Unreviewed;       320 AA.
AC   D4N133;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   28-FEB-2018, entry version 41.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CL2_16520 {ECO:0000313|EMBL:CBL38578.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38578.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL38578.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38578.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL38578.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38578.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929061; CBL38578.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4N133; -.
DR   EnsemblBacteria; CBL38578; CBL38578; CL2_16520.
DR   KEGG; bprl:CL2_16520; -.
DR   PATRIC; fig|245018.3.peg.1946; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   Proteomes; UP000008960; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:CBL38578.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008960};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CBL38578.1};
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:UP000008960};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   320 AA;  35577 MW;  3D350F4364F4890D CRC64;
     MIPETWFDRP LSVAGRIIIE ENGQIKDQLV NVDRDLMIIP NLAIHMSRSS NESKQLNPQK
     DLLPLCGGNL TKDGFEEMIA KESGVEKEDI LSYDLFLYNR MRGTTLGINE EFVAAPKLDD
     LECAYSSIEG MLNAKLSKDY VTVCAVFDNE EVGSGTKQGA GSTFFPEVLK RISYLCGKNE
     EEYYMAVADS FMLSADNAHA VHPNYQDKTD PTNRPYINEG IVLKYNASQK YTTDANSAAL
     VKYLCKKEKI KCQVFFNRSD MLGGSTLGNI LTGQVSIKAA DIGLPQLSMH STYETAGCKD
     LDDMITLMGS FYELGKEVQI
//
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