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Database: UniProt
Entry: A0A1H5MIR1_9ACTN
LinkDB: A0A1H5MIR1_9ACTN
Original site: A0A1H5MIR1_9ACTN 
ID   A0A1H5MIR1_9ACTN        Unreviewed;       432 AA.
AC   A0A1H5MIR1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-MAR-2018, entry version 5.
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=SAMN05216533_4215 {ECO:0000313|EMBL:SEE89295.1};
OS   Streptomyces sp. Ag109_O5-10.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE89295.1, ECO:0000313|Proteomes:UP000198812};
RN   [1] {ECO:0000313|EMBL:SEE89295.1, ECO:0000313|Proteomes:UP000198812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE89295.1,
RC   ECO:0000313|Proteomes:UP000198812};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNTQ01000001; SEE89295.1; -; Genomic_DNA.
DR   Proteomes; UP000198812; 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   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:SEE89295.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198812};
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:UP000198812};
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;  45697 MW;  002A79AF4D05ABF9 CRC64;
     MSEPSRFDRG HTDDLMSFLA AGPTPYHAVA SAAARLEKAG FRQVAETDAW DGTAGGKFVL
     RGGAIIAWYV PEGAAPHTPF RIVGAHTDSP NLRVKPRPDT GAHGFRQVAV EIYGGPLMNS
     WLDRDLGLAG RLSLRDGSTR LVDVNRPLLR VPQLAIHLDR SVSSEGLKLD KQRHLQPIWG
     LGDDVRDGDL IAFLEQESGL PAGSVTGWDL MTYTVEPPAY LGRDQDLMAG PRMDNLLSVH
     AGTAALAAVA TGGADLPCIP VLAAFDHEET GSQSDTGADG PLLGSVMERS VLARGGSFED
     RARAFAGSVC LSSDTGHAVH PNYAERHDPT HHPRLNGGPI LKVNVNNRYA TDGSGRAVFA
     AACEKAGVPF QTFVSNNSMP CGTTIGPITA ARHGIRTVDI GAAILSMHSA RELCGADDPF
     LLANALVAFL EG
//
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