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Database: UniProt
Entry: A0A0J6ZRW4_9FIRM
LinkDB: A0A0J6ZRW4_9FIRM
Original site: A0A0J6ZRW4_9FIRM 
ID   A0A0J6ZRW4_9FIRM        Unreviewed;       455 AA.
AC   A0A0J6ZRW4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=AB840_00750 {ECO:0000313|EMBL:KMO87696.1};
OS   Megasphaera cerevisiae DSM 20462.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO87696.1, ECO:0000313|Proteomes:UP000036503};
RN   [1] {ECO:0000313|EMBL:KMO87696.1, ECO:0000313|Proteomes:UP000036503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO87696.1,
RC   ECO:0000313|Proteomes:UP000036503};
RA   Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A.,
RA   Han S., Martens-Habbena W., Neal-McKinney J., Janagama H.K.,
RA   Nadala C., Samadpour M.;
RT   "Draft genome sequence of beer spoilage bacterium Megasphaera
RT   cerevisiae type strain 20462.";
RL   Submitted (JUN-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:KMO87696.1}.
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DR   EMBL; LEKT01000002; KMO87696.1; -; Genomic_DNA.
DR   RefSeq; WP_048512918.1; NZ_LEKT01000002.1.
DR   EnsemblBacteria; KMO87696; KMO87696; AB840_00750.
DR   PATRIC; fig|1122219.3.peg.166; -.
DR   Proteomes; UP000036503; 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:KMO87696.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036503};
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:UP000036503};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   455 AA;  50540 MW;  3A63C40E5D94BDDF CRC64;
     MKAFDMENSV WARFSEEERL EMEEYNQKYR QFLDTARTER LAAREILRQA EAAGFRPLGD
     YTELKAGDKV YWNQKGKSVI LAVIGTDPID RGMKIVGSHI DCPRLDLKAM PVIEKNKIVY
     FKTHYYGGIL KYQWVCMPLS LIGIVYTTDG RQIDISIGED PADPVFYIND LLPHLGKDQA
     AKKLNEAITG EMLMPIVGTY SQEEKTKPAI LTLLKNKYGI EEEDFASAEL EIIPAQKSRE
     VGLDRSMIMS HGHDDRVCSY GNLAAILYAK AGTKTQAALF ADKEEIGSVG NTGVQSSYFL
     DFTAELLALQ GRTEELYLRR TLRSSEVLSA DVCAALDPVF PDAYEESNAA KLGYGICLCK
     YTGARGKSGS NDANAEYLSK IRQLFNTHNV PWQIGELGKV DQGGGGTIAY IMADWGCDVV
     DCGVAMLSMH APLEIVAKTD AYSGYLAYKA FFESK
//
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