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Database: UniProt
Entry: A0A1H4VW40_9ACTN
LinkDB: A0A1H4VW40_9ACTN
Original site: A0A1H4VW40_9ACTN 
ID   A0A1H4VW40_9ACTN        Unreviewed;       431 AA.
AC   A0A1H4VW40;
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=SAMN05216482_4869 {ECO:0000313|EMBL:SEC84708.1};
OS   Streptomyces sp. PAN_FS17.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1855351 {ECO:0000313|EMBL:SEC84708.1, ECO:0000313|Proteomes:UP000199275};
RN   [1] {ECO:0000313|EMBL:SEC84708.1, ECO:0000313|Proteomes:UP000199275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAN_FS17 {ECO:0000313|EMBL:SEC84708.1,
RC   ECO:0000313|Proteomes:UP000199275};
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; FNTN01000001; SEC84708.1; -; Genomic_DNA.
DR   RefSeq; WP_030951255.1; NZ_FNTN01000001.1.
DR   Proteomes; UP000199275; 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:SEC84708.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199275};
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:UP000199275};
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;  45689 MW;  C05E8CADBB609FEC CRC64;
     MSEPPRFDRG HTDDLMSFLA ASPSPYHAVA NAAERLEKAG FRQVAETDAW DGTSGGKYVL
     RGGAIVAWYV PEGAAPHTPF RIVGAHTDSP NLRVKPLPDT GAHGWRQVAV EIYGGPLLNS
     WLDRDLGLAG RLTLRDGTTR LVNVDRPLLR VPQLAIHLDR SVSAEGLKLD KQRHLQPVWG
     LGDTRDGDLI AFLEETAGLA AGEVAGWDLM AHSIEAPAYL GRDNELMAGP RMDNLLSVHA
     GAAALAAVAG SGAALPCIPV LAAFDHEENG SQSDTGADGP LLGSVLERSV FARGGSYEDR
     ARAFAGTVCL SSDTGHAVHP NYAERHDPTH HPRVNGGPIL KVNVNNRYAT DGSGRAVWAA
     ACEKAEVPFQ SFVSNNSMPC GTTIGPITAA RHGIKTVDIG VAILSMHSAR ELCGADDPWL
     LTNSLVAFLE G
//
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