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Database: UniProt
Entry: A0A0M9ZLY8_9ACTN
LinkDB: A0A0M9ZLY8_9ACTN
Original site: A0A0M9ZLY8_9ACTN 
ID   A0A0M9ZLY8_9ACTN        Unreviewed;       432 AA.
AC   A0A0M9ZLY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 8.
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=ADK64_20715 {ECO:0000313|EMBL:KOV63516.1};
OS   Streptomyces sp. MMG1121.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV63516.1, ECO:0000313|Proteomes:UP000037687};
RN   [1] {ECO:0000313|EMBL:KOV63516.1, ECO:0000313|Proteomes:UP000037687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1121 {ECO:0000313|EMBL:KOV63516.1,
RC   ECO:0000313|Proteomes:UP000037687};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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}.
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:KOV63516.1}.
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DR   EMBL; LGDV01000190; KOV63516.1; -; Genomic_DNA.
DR   RefSeq; WP_053661070.1; NZ_LGDV01000190.1.
DR   EnsemblBacteria; KOV63516; KOV63516; ADK64_20715.
DR   PATRIC; fig|1415544.3.peg.4457; -.
DR   Proteomes; UP000037687; Unassembled WGS sequence.
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:KOV63516.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037687};
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   Reference proteome {ECO:0000313|Proteomes:UP000037687};
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       408    408       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   432 AA;  45860 MW;  2A062797B405A661 CRC64;
     MSAPARFDRG HTDDLMSFLA AGPSPYHAVA ATAERLEKAG FRQVAETDAW DGTTGGKYVL
     RGGAIVAWYV PEGAEPHTPF HIVGAHTDSP NLRVKPRPDS GAHGWRQVAV ELYGGPLMNS
     WLDRDLGLAG RLTLRDGSSV LVNVDRPLLR VPQLAIHLDR SVSTEGLKLD KQRHLQPVWG
     LGDDVREGDL IGFLEQEAGL AAGSVAGWDL MVHPVEPPAY LGRDRELLAG PRMDNLLSVH
     AATAALASAV TSGAPLAHIP VLAAFDHEEN GSQSDTGADG PLLGSVLERS VFARGGSWED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVNGGPI LKVNVNNRYA TDGSGRAIFA
     AACEKANVPF QSFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGADDPY
     LLANALVAFL EG
//
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