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Database: UniProt
Entry: A0A0D4DQM5_9ACTN
LinkDB: A0A0D4DQM5_9ACTN
Original site: A0A0D4DQM5_9ACTN 
ID   A0A0D4DQM5_9ACTN        Unreviewed;       431 AA.
AC   A0A0D4DQM5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 11.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=T261_4233 {ECO:0000313|EMBL:AJT65887.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AJT65887.1, ECO:0000313|Proteomes:UP000032413};
RN   [1] {ECO:0000313|Proteomes:UP000032413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A02 {ECO:0000313|Proteomes:UP000032413};
RA   Wu H., Yan J., Liu W., Liu T., Dong D., Li J., Liu H., Lu C.,
RA   Zhang D., Zhang T., Tian Z.;
RT   "Complete genome sequence of the natamycin-producing actinomycete
RT   Streptomyces lydicus A02.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP007699; AJT65887.1; -; Genomic_DNA.
DR   RefSeq; WP_046927141.1; NZ_CP007699.2.
DR   EnsemblBacteria; AJT65887; AJT65887; T261_4233.
DR   KEGG; sld:T261_4233; -.
DR   PATRIC; fig|1403539.3.peg.4381; -.
DR   KO; K01267; -.
DR   Proteomes; UP000032413; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:AJT65887.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032413};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       407    407       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   431 AA;  45748 MW;  FA65EB1D573C0B45 CRC64;
     MSNSSRFDRG HTDDLMSFLA ASPSPYHAVA NAAERLEKAG FRQVAETDAW DGSSGGKYVL
     RGGAIIAWYV PEGASAATPY RIVGAHTDSP NLRVKPIPDT GARGWRQIAV EIYGGTLLNT
     WLDRDLGLSG RVTLKDGNHR LVNVDRALLR VPQLAVHLDR SVNTDGLKLD KQRHMTPIWG
     LGEVAEGDLI SFVEEEIGVA PGTVRGWDLM VHSIEPPAYL GRDQELVAGP RMDNLLSVHA
     GTAALTAAAA AGSALTTIPV LAAFDHEENG SQSDTGADGP LLGTVLERSV FARGGSYEDR
     ARAFAGTVCL SSDTGHAVHP NYSERHDPGH HPMPNGGPIL KVNVNQRYAT DGSGRAVFAA
     ACERADVPWQ SFVSNNSMPC GTTIGPITAA RHGITTVDIG VAILSMHSAR ELCGAKDPYL
     LANALTAFLE G
//
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