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Database: UniProt
Entry: A0A140L9E6_9CLOT
LinkDB: A0A140L9E6_9CLOT
Original site: A0A140L9E6_9CLOT 
ID   A0A140L9E6_9CLOT        Unreviewed;       475 AA.
AC   A0A140L9E6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 8.
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:KXG77171.1};
GN   ORFNames=AN619_07010 {ECO:0000313|EMBL:KXG77171.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG77171.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG77171.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG77171.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea
RT   metallivorans, an isolate from the runoff channel of the Great
RT   Artesian Basin, Australia.";
RL   Submitted (DEC-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:KXG77171.1}.
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DR   EMBL; LOEE01000019; KXG77171.1; -; Genomic_DNA.
DR   RefSeq; WP_068555077.1; NZ_LOEE01000019.1.
DR   EnsemblBacteria; KXG77171; KXG77171; AN619_07010.
DR   PATRIC; fig|520762.4.peg.782; -.
DR   Proteomes; UP000070456; 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   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:KXG77171.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070456};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KXG77171.1};
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:UP000070456};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   475 AA;  52647 MW;  77108A649764E6B3 CRC64;
     MTEQTKIQEC QDRIIYEFKN GWDQLSADER EKVYALNDVY KQFLDKGKTE RECIEEIIRL
     AEERGFVNIA DVIKGKIEVK EGLKVYANNK GKAAALFILG KEALEYGMNI VGAHVDVPRL
     DLKPFPLYED GGLALLKTHY YGGIKKYQWT AIPLALHGVV TRKDGKKLRI VIGEDENDPT
     FFITDLLPHL SKDQIEKKLS EGITGEGLNV LIGSIPYEDA SVKERVKYQV MKLLHEKYGI
     EEDDFLVAEI EVVPAGKARD VGIDRSMVGA YGHDDRVCSF AALQAIVEME NPVRTAVALF
     VDKEEVGSMG NTGMESRFFE NAVAELIAAQ SKDYSELKVR RAMANSKVLS GDVGAGFDPN
     FPDVMDKRNA AFLGKGVILV KYTGVRGKSG SNDANAEFLA EVRRIFHDNG VIWQIGELGK
     VDQGGGGTIA YILANYGAEV VDCGVPVLSM HAPMEIVSKV DVYMTYKAYK AFFKA
//
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