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Database: UniProt
Entry: A0A0F0CES0_9CLOT
LinkDB: A0A0F0CES0_9CLOT
Original site: A0A0F0CES0_9CLOT 
ID   A0A0F0CES0_9CLOT        Unreviewed;       442 AA.
AC   A0A0F0CES0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeB {ECO:0000313|EMBL:KJJ71267.1};
GN   ORFNames=CLFS41_26510 {ECO:0000313|EMBL:KJJ71267.1};
OS   Clostridium sp. FS41.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ71267.1, ECO:0000313|Proteomes:UP000033604};
RN   [1] {ECO:0000313|EMBL:KJJ71267.1, ECO:0000313|Proteomes:UP000033604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS41 {ECO:0000313|EMBL:KJJ71267.1,
RC   ECO:0000313|Proteomes:UP000033604};
RA   Poehlein A., Daniel R.;
RT   "Genome sequencing of Clostridium sp. FS41.";
RL   Submitted (FEB-2015) 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:KJJ71267.1}.
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DR   EMBL; JYHN01000059; KJJ71267.1; -; Genomic_DNA.
DR   RefSeq; WP_007858169.1; NZ_JYHN01000059.1.
DR   EnsemblBacteria; KJJ71267; KJJ71267; CLFS41_26510.
DR   PATRIC; fig|1609975.3.peg.2854; -.
DR   Proteomes; UP000033604; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KJJ71267.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033604};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KJJ71267.1};
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:UP000033604};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   442 AA;  48720 MW;  61852E8D1EA345D5 CRC64;
     MTLDRNDCRK TAEGLIRFLE DSPTSFHAVE NIGRLLCEAG FTQLHEGEAW ELRRGGSYFV
     TRNQSSILSF KIPLGAFNGF HLIASHSDSP SFKIKENPEM EAGGHYIKLN VEKYGGMLCA
     PWMDRPLSVA GRLVVREGKR LVTKLVKVDR DLLMIPNLAI HFNREVNDGY KYNPQVDMLP
     LYGDASAKGT FMKTVAESAG VREEDVLGHD LFLYSRTPGT IWGADGEFIS CGRLDDLQCA
     FASLKGFLEG ENSENVSVHA VFDNEEVGSG TKQGADSTFL EDTLKRINRN LGRSEEEYLM
     SLASSFMISA DNAHAVHPNL DLKADPTNRP YMNEGIVIKY NANQKYTTDA VSAAMFKVLC
     QEADVPFQTF ANRSDMPGGS TLGNISNAHV ALNTVDIGLP QLAMHSPYET AGIKDTCYLV
     QVAKHFYSAG IRAGESGSYE II
//
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