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Database: UniProt
Entry: A0A151B539_9CLOT
LinkDB: A0A151B539_9CLOT
Original site: A0A151B539_9CLOT 
ID   A0A151B539_9CLOT        Unreviewed;       473 AA.
AC   A0A151B539;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-NOV-2017, entry version 9.
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:KYH35034.1};
GN   ORFNames=CLTEP_10270 {ECO:0000313|EMBL:KYH35034.1};
OS   Clostridium tepidiprofundi DSM 19306.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH35034.1, ECO:0000313|Proteomes:UP000075531};
RN   [1] {ECO:0000313|EMBL:KYH35034.1, ECO:0000313|Proteomes:UP000075531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH35034.1,
RC   ECO:0000313|Proteomes:UP000075531};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL   Submitted (FEB-2016) 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:KYH35034.1}.
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DR   EMBL; LTBA01000007; KYH35034.1; -; Genomic_DNA.
DR   RefSeq; WP_066823522.1; NZ_LTBA01000007.1.
DR   EnsemblBacteria; KYH35034; KYH35034; CLTEP_10270.
DR   PATRIC; fig|1121338.3.peg.1059; -.
DR   Proteomes; UP000075531; 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:KYH35034.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075531};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KYH35034.1};
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:UP000075531};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   473 AA;  52539 MW;  4CFFFBE01228C822 CRC64;
     MTEEKKNNKT NFEKKYELAW DKYSKEDLKK VYDLSDEYIN FMSICKTERE CVTEFIKRAE
     KFGYRDINSV IAEGKGVKAG DKIYANCMGK TLALFLIGSE PIEKGLKILG AHVDSPRLDL
     KQNPLYEDSD LALLKTHYYG GVKKYQWVTI PLAIHGVVVK KDGSIVNIVI GEDESEPVVG
     ISDLLIHLSA DQMQKTLAKG IEGESLNVCF GSLPIEDKDE KERVKKNILK LMNDKYGIVE
     EDFVSAELEV VPAGRARSYG LDGSMVMAYG HDDRICSYTS FEAMMTLNST DKTCVTLLVD
     KEEVGSIGAT GMQSKFFENT VAEIINLMGD YSDIKLKRAL ANSKMLSSDV SAAFDPNYPS
     VMEKRNSAFF GKGIVFNKYT GARGKGGCND ANPEFIAELR AIMEKHNVSW QTAELGKVDQ
     GGGGTIAYIL AQYGMQVIDS GVALHNMHAP WEIASKADIY EAYRAYKAFL IEA
//
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