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Database: UniProt
Entry: A0A0L0WDD9_CLOPU
LinkDB: A0A0L0WDD9_CLOPU
Original site: A0A0L0WDD9_CLOPU 
ID   A0A0L0WDD9_CLOPU        Unreviewed;       475 AA.
AC   A0A0L0WDD9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 10.
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:KNF09482.1};
GN   ORFNames=CLPU_3c02620 {ECO:0000313|EMBL:KNF09482.1};
OS   Clostridium purinilyticum (Gottschalkia purinilyticum).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1503 {ECO:0000313|EMBL:KNF09482.1, ECO:0000313|Proteomes:UP000037267};
RN   [1] {ECO:0000313|Proteomes:UP000037267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1384 {ECO:0000313|Proteomes:UP000037267};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA   Duerre P.;
RT   "Draft genome sequence of the purine-degrading Gottschalkia
RT   purinilyticum DSM 1384 (formerly Clostridium purinilyticum).";
RL   Submitted (JUL-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:KNF09482.1}.
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DR   EMBL; LGSS01000003; KNF09482.1; -; Genomic_DNA.
DR   RefSeq; WP_050354464.1; NZ_LGSS01000003.1.
DR   EnsemblBacteria; KNF09482; KNF09482; CLPU_3c02620.
DR   PATRIC; fig|1503.3.peg.2131; -.
DR   Proteomes; UP000037267; 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:KNF09482.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037267};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KNF09482.1};
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:UP000037267};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   475 AA;  52908 MW;  9F43715C60EF9939 CRC64;
     MNKKLRGKEL KEKLTHTWPN VWENTDDTQK DMIFGLGDEY KSFLDKSKTE REAVSEIIKI
     AEENGYISLE TIINKNIKVV PGTKIYANNK GKSIALFVIG KESLEKGMHI VGSHVDAPRI
     DLKQFPLYED SNLAFLKTHY YGGIKKYQWV TLPLALHGVV IKSNGEKEYI VIGEDEKDPV
     FFITDLLPHL AKDQMSKKLD EAIVGEGLNI LIGSIPYNDD EISEKVKLNI LNVLYEKYGI
     VEEDFTTAEF EIVPAGKARD VGIDRSMIGG YGQDDRVCVF TSLKAILETE CPNKTAVGLF
     MDKEEVGSLG NTGMESKFFE NVVSELINLT EENYSELIVK RSLANSKVLS ADTVGAFDPN
     YPDVLDKRNS PFLGKGICLV KYTGVKGKSS SNDANSEYIS YIRDIFNKNN VIWQMGELGK
     VDQGGGGTIA YILANYGMEV VDCGVALLSV HGPFEISSKA DVYMAYEGYK AFYKS
//
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