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Database: UniProt
Entry: A0A0F0C5T7_9CLOT
LinkDB: A0A0F0C5T7_9CLOT
Original site: A0A0F0C5T7_9CLOT 
ID   A0A0F0C5T7_9CLOT        Unreviewed;       464 AA.
AC   A0A0F0C5T7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeA {ECO:0000313|EMBL:KJJ68557.1};
GN   ORFNames=CLFS41_46220 {ECO:0000313|EMBL:KJJ68557.1};
OS   Clostridium sp. FS41.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ68557.1, ECO:0000313|Proteomes:UP000033604};
RN   [1] {ECO:0000313|EMBL:KJJ68557.1, ECO:0000313|Proteomes:UP000033604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS41 {ECO:0000313|EMBL:KJJ68557.1,
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:KJJ68557.1}.
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DR   EMBL; JYHN01000069; KJJ68557.1; -; Genomic_DNA.
DR   RefSeq; WP_007865969.1; NZ_JYHN01000069.1.
DR   EnsemblBacteria; KJJ68557; KJJ68557; CLFS41_46220.
DR   PATRIC; fig|1609975.3.peg.4941; -.
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:KJJ68557.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033604};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KJJ68557.1};
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   464 AA;  51270 MW;  5B9C8538918A38D8 CRC64;
     MAKKTKAQEL REELTWSFPH IAKDAPEQVE KAFGYCEGYK AFLDGGKTER ECVKAGIKML
     KKAGYKPFDR KASYEPGDKV YYVNRGKALI ATTFGRKPLT EGVRINGAHI DSPRLDLKPN
     PLYEKEEIAY FKTHYYGGIR KYQWGTIPLA IHGVVVKKNG ETVEVCIGEK ESDPVFCVTD
     LLPHLSAKQN ERPLKDGLKG EELNIVVGSL PFQDEEIKEP FKLLALSLLN ERYGITEKDF
     FRAELELVPA VKARDVGLDA SMIGAYGQDD RVCAYTALTA EIDAKKPAHT TITILTDKEE
     TGSDGNTGLN SDYVLHYIED LADQAGVKVR DILRNSLCLS SDVNAAYDPT FPDVYESRNS
     SYVNKGCVLT KYTGARGKSG SNDASAEVMA KVISMMEQEG VYWQAGELGA VDAGGGGTIA
     KFVAHMNVDT VDLGVPILSM HSPFELASKL DVYNTYKAFR AFYK
//
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