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Database: UniProt
Entry: A0A124EG57_9FIRM
LinkDB: A0A124EG57_9FIRM
Original site: A0A124EG57_9FIRM 
ID   A0A124EG57_9FIRM        Unreviewed;       455 AA.
AC   A0A124EG57;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-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   ORFNames=AT798_01390 {ECO:0000313|EMBL:KUH56469.1};
OS   Megasphaera sp. DJF_B143.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=537288 {ECO:0000313|EMBL:KUH56469.1, ECO:0000313|Proteomes:UP000054462};
RN   [1] {ECO:0000313|EMBL:KUH56469.1, ECO:0000313|Proteomes:UP000054462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJF_B143 {ECO:0000313|EMBL:KUH56469.1,
RC   ECO:0000313|Proteomes:UP000054462};
RA   Li X., Marshall I.P., Schreiber L., Canibe N., Jensen B.;
RT   "Draft genome sequence of Megasphaera sp. strain DJF_B143, isolated
RT   from pig hind-gut.";
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:KUH56469.1}.
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DR   EMBL; LODR01000012; KUH56469.1; -; Genomic_DNA.
DR   RefSeq; WP_059076183.1; NZ_LODR01000012.1.
DR   EnsemblBacteria; KUH56469; KUH56469; AT798_01390.
DR   Proteomes; UP000054462; 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:KUH56469.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054462};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
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:UP000054462};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   455 AA;  50070 MW;  8687D4B8F0DC28DE CRC64;
     MKAFDRENSV WARFSEEQRL EMEEYSKKYR QFLDTARTER LANAEIIRQA EAAGFRPLSD
     YTSLKAGDKV YWNQKGKSVI LAVIGTEPVS QGMKIVGSHI DCPRLDLKAM PVTEKNGIVY
     FKTHYYGGLL KYQWVCLPLS LIGVVYTADG RRIDVSIGED PDDPVFFIND LLPHLGKDQA
     AKKLSEAISG EMLMPLVGTN SEEEKTKPAV LELLKKKYGI EEEDFASAEL EIIPAIKSRD
     VGLDRSMIMS HGHDDRVCSY GNLAAILTAH AGTKTQVALF ADKEEIGSVG NTGVHSAFFP
     DFVAELLALQ GHTEELWLRR AMRNSQVLSA DVCAALDPVF ADAYEETNAA RLGYGICLCK
     YTGARGKAGS NDANAEFLSQ VRQIFNAADV PWQIGELGKV DQGGGGTIAY IMADWGCDVV
     DCGVAMHSMH APLEIVAKSD AYSGYLAYKA FFESK
//
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