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Database: UniProt
Entry: E7KPG2_YEASL
LinkDB: E7KPG2_YEASL
Original site: E7KPG2_YEASL 
ID   E7KPG2_YEASL            Unreviewed;       482 AA.
AC   E7KPG2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   12-APR-2017, entry version 20.
DE   SubName: Full=YHR113W-like protein {ECO:0000313|EMBL:EGA82524.1};
GN   ORFNames=QA23_2170 {ECO:0000313|EMBL:EGA82524.1};
OS   Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764098 {ECO:0000313|EMBL:EGA82524.1, ECO:0000313|Proteomes:UP000007236};
RN   [1] {ECO:0000313|EMBL:EGA82524.1, ECO:0000313|Proteomes:UP000007236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin QA23 {ECO:0000313|EMBL:EGA82524.1,
RC   ECO:0000313|Proteomes:UP000007236};
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that
RT   characterize the genome of industrial strains of Saccharomyces
RT   cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {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:EGA82524.1}.
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DR   EMBL; ADVV01000041; EGA82524.1; -; Genomic_DNA.
DR   EnsemblFungi; EGA82524; EGA82524; QA23_2170.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007236; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007236};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007236};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   482 AA;  53127 MW;  575E8B8CB3EFCE3B CRC64;
     MSSKTCKSDY PKEFVSFLNS SHSPYHTVHN IKKHLVSNGF KELSERDSWA GHVAQKGKYF
     VTRNGSSIIA FAVGGKWEPG NPIAITGAHT DSPALRIKPI SKRVSEKYLQ VGVETYGGAI
     WHSWFDKDLG VAGRVFVKDA KTGKSIARLV DLNRPLLKIP TLAIHLDRDV NQKFEFNRET
     QLLPIGGLQE DKTEAKTEKE INNGEFTSIK TIVQRHHAEL LGLIAKELAI DTIEDIEDFE
     LILYDHNAST LGGFNDEFVF SGRLDNLTSC FTSMHGLTLA ADTEIDRESG IRLMACFDHE
     EIGSSSAQGA DSNFLPNILE RLSILKGDGS DQTKPLFHSA ILETSAKSFF LSSDVAHAVH
     PNYANKYESQ HKPLLGGGPV IKINANQRYM TNSPGLVLVK RLAEAAKVPL QLFVVANDSP
     CGSTIGPILA SKTGIRTLDL GNPVLSMHSI RETGGSADLE FQIKLFKEFF ERYTSIESEI
     VV
//
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