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Database: UniProt
Entry: A0A0F4KAC9_9ACTN
LinkDB: A0A0F4KAC9_9ACTN
Original site: A0A0F4KAC9_9ACTN 
ID   A0A0F4KAC9_9ACTN        Unreviewed;       431 AA.
AC   A0A0F4KAC9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-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=VR41_05535 {ECO:0000313|EMBL:KJY42953.1};
OS   Streptomyces sp. NRRL B-1568.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609106 {ECO:0000313|EMBL:KJY42953.1, ECO:0000313|Proteomes:UP000053394};
RN   [1] {ECO:0000313|EMBL:KJY42953.1, ECO:0000313|Proteomes:UP000053394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-1568 {ECO:0000313|EMBL:KJY42953.1,
RC   ECO:0000313|Proteomes:UP000053394};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJY42953.1}.
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DR   EMBL; JZWZ01000039; KJY42953.1; -; Genomic_DNA.
DR   RefSeq; WP_045932973.1; NZ_JZWZ01000039.1.
DR   EnsemblBacteria; KJY42953; KJY42953; VR41_05535.
DR   PATRIC; fig|1609106.3.peg.1498; -.
DR   Proteomes; UP000053394; 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:KJY42953.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053394};
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:UP000053394};
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;  45686 MW;  5FA9A6757F644BB7 CRC64;
     MSSAHRFDRG HTDDLMTFLA ASPSPYHAVA EAAERLEKAG FRQVAETDAW DASAGGKYVL
     RGGAIIAWFV PEEASAATPF RIVGAHTDSP NLRVKPLPDT GAQGWRQVAV EIYGGTLLNT
     WLDRDLGLSG RITLRDGSHR LVNVDRPLLR VPQLAIHLDR GVNADGLKLD KQRHMTPIWG
     LGEVGEGDLI SFVAEETGVD AAEIGGWDLM VHSVEAPAYL GRDQELLAGP RMDNLLSVHA
     GVAALIAASR PGAALTSIPV LAAFDHEENG SQSDTGAEGP LLGNVLERSV FARGGSYEDK
     ARAFAGTVCL SSDTGHAVHP NYSERHEPGH HPMPNGGPIL KVNVNQRYAT DGSGRAVFAA
     ACERAGVPWQ HFVSNNSMPC GTTIGPITAA RHGITTVDIG VAILSMHSAR ELCGADDPHL
     LASALTAFLE G
//
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