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Database: UniProt
Entry: J8PLG7_SACAR
LinkDB: J8PLG7_SACAR
Original site: J8PLG7_SACAR 
ID   J8PLG7_SACAR            Unreviewed;       514 AA.
AC   J8PLG7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   10-MAY-2017, entry version 24.
DE   SubName: Full=Lap4p {ECO:0000313|EMBL:EJS42965.1};
GN   ORFNames=SU7_1969 {ECO:0000313|EMBL:EJS42965.1};
OS   Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS42965.1, ECO:0000313|Proteomes:UP000006968};
RN   [1] {ECO:0000313|EMBL:EJS42965.1, ECO:0000313|Proteomes:UP000006968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-6 / AS 2.3317 / CBS 10644
RC   {ECO:0000313|Proteomes:UP000006968};
RX   PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA   Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA   Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA   Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT   "High quality de novo sequencing and assembly of the Saccharomyces
RT   arboricolus genome.";
RL   BMC Genomics 14:69-69(2013).
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:EJS42965.1}.
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DR   EMBL; ALIE01000126; EJS42965.1; -; Genomic_DNA.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EJS42965; EJS42965; SU7_1969.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000006968; Chromosome XI.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
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:UP000006968};
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:UP000006968};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   514 AA;  56752 MW;  5695A45495EA8DE9 CRC64;
     MEEQRAILEQ LKQTLQMLTV ESSKNDGSAN EQNEKKNIED SECILEREYE DIAQEFIDFI
     YNNPTTYHVV SFFGKLLDKN GFQYLSEKSD WSDSIGEKGG KFYTTRNGTN LSAFILGKNW
     KAEKGVGVIG SHVDALTVKL KPVSFKDPSE GYGRIAVAPY GGTLNELWLD RDLGIGGRVL
     YKKKGSNVIK STLIDSTPYP ICKIPSLAPH FGKPAEGPFD KEDQTVPVIG FPTSHGKDKE
     IPTDDEKKSP LYGKHCLHLL RYIAKLAGVK VSELIQTDLD LFDVQKGTIG GIRKHFIFAP
     RLDDRLCSFA AMIALISYAK NVNTDDSDLF STVTLYDNEE IGSLTRQGAK GGLLESVVQR
     SSSAFSKEPV DLHTVWANSI ILSADVNHLL NPNFSEVYLK NHSPVPNVGI TLSLDPNGHM
     ATDVVGTALV EELARRNGDK VQYFQIKNNS RSGGTIGPSL ASQTGARTID LGIAQLSMHS
     IRATTGSMDV ALGVKFFDGF FRNWRSVYDE FGEF
//
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