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Database: UniProt
Entry: V6K2W4_9ACTN
LinkDB: V6K2W4_9ACTN
Original site: V6K2W4_9ACTN 
ID   V6K2W4_9ACTN            Unreviewed;       433 AA.
AC   V6K2W4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 20.
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=N566_23785 {ECO:0000313|EMBL:EST26550.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST26550.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST26550.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST26550.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J.,
RA   Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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:EST26550.1}.
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DR   EMBL; AWQV01000777; EST26550.1; -; Genomic_DNA.
DR   RefSeq; WP_023531431.1; NZ_KI547050.1.
DR   EnsemblBacteria; EST26550; EST26550; N566_23785.
DR   PATRIC; fig|1380770.3.peg.4141; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000017915; 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:EST26550.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017915};
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:UP000017915};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        87     87       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       158    158       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       409    409       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   433 AA;  45989 MW;  72D077727C8F74E2 CRC64;
     MSNAPHRFDR GHTDDLTTFL TRSPTPYHAV ASAARMLEKA GFRQVEETAA WDGEAGGRYV
     LRGGAIIAWY VPEGATPATP YRIVGAHTDS PNLRVKPLPD TGANGWRQVA VEVYGGTLLN
     TWLDRDLGLA GRLTLRDGTT RLVNVDRPLL RVPQLAIHLD RQVNEGLKLD KQRHMTPVWG
     LGTPEEGDLI AFLADEAGLN ADDVTGWDLM VHSVEAPAYL GADRELLAGP RMDNLMSVHA
     GAAALAAVAG ESGGSALNFV PVLAAFDHEE NGSQSDTGAD GPLLGNVLER SVFARGGTYE
     DRARAYAGTV CLSSDTGHAV HPNYAERHEP GHHPMPNGGP ILKVNVNQRY ATDGTGRAVF
     AAACERAGVP WQNFVSNNAM PCGTTIGPIT AARHGISTID IGVAILSMHS ARELCGADDP
     HMLASALAAF LAD
//
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