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Database: UniProt
Entry: E7QH69_YEASZ
LinkDB: E7QH69_YEASZ
Original site: E7QH69_YEASZ 
ID   E7QH69_YEASZ            Unreviewed;       514 AA.
AC   E7QH69;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   12-APR-2017, entry version 25.
DE   SubName: Full=Lap4p {ECO:0000313|EMBL:EGA85909.1};
GN   ORFNames=VL3_2860 {ECO:0000313|EMBL:EGA85909.1};
OS   Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764100 {ECO:0000313|EMBL:EGA85909.1, ECO:0000313|Proteomes:UP000007238};
RN   [1] {ECO:0000313|EMBL:EGA85909.1, ECO:0000313|Proteomes:UP000007238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zymaflore VL3 {ECO:0000313|Proteomes:UP000007238};
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:EGA85909.1}.
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DR   EMBL; AEJS01000045; EGA85909.1; -; Genomic_DNA.
DR   ProteinModelPortal; E7QH69; -.
DR   EnsemblFungi; EGA85909; EGA85909; VL3_2860.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007238; Unassembled WGS sequence.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05639; M18; 1.
DR   InterPro; IPR033818; Aminopeptidase_I.
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:UP000007238};
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:UP000007238};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   514 AA;  57068 MW;  B6C1CD5CE930D35F CRC64;
     MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE DIAQEFIDFI
     YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG KFYTIRNGTN LSAFILGKNW
     RAEKGVGVIG SHVDALTVKL KPVSFKDTAE GYGRIAVAPY GGTLNELWLD RDLGIGGRLL
     YKKKGTNEIK SALVDSTPLP VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPSPDEEGNE
     PPTDDEKKSP LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP
     RLDDRLCSFA AMIALICYAK DVDTEESELF STVTLYDNEE IGSLTRQGAK GGLLESVVER
     SSSAFTKKAV DLHTVWANSI ILSADVNHLY NPNFPEVYLK NHFPVPNVGI TLSLDPNGHM
     ATDVVGTALV EELARRNGDK VQYFQIKNNS RSGGTIGPSL ASQTGARTID LGIAQLSMHS
     IRAATGSKDV GLGVKFFNGF FKHWRSVYDE FGEL
//
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