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YPI1_PICGU
ID   YPI1_PICGU              Reviewed;         117 AA.
AC   A5DNZ1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Type 1 phosphatases regulator YPI1;
GN   Name=YPI1; ORFNames=PGUG_04992;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Regulator of type 1 phosphatases which maintains protein
CC       phosphatase activity under strict control. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}.
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DR   EMBL; CH408160; EDK40894.2; -; Genomic_DNA.
DR   RefSeq; XP_001483037.1; XM_001482987.1.
DR   AlphaFoldDB; A5DNZ1; -.
DR   SMR; A5DNZ1; -.
DR   STRING; 4929.XP_001483037.1; -.
DR   EnsemblFungi; EDK40894; EDK40894; PGUG_04992.
DR   GeneID; 5124850; -.
DR   KEGG; pgu:PGUG_04992; -.
DR   VEuPathDB; FungiDB:PGUG_04992; -.
DR   eggNOG; KOG4102; Eukaryota.
DR   HOGENOM; CLU_098333_3_0_1; -.
DR   InParanoid; A5DNZ1; -.
DR   OrthoDB; 1626526at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PTHR20835; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..117
FT                   /note="Type 1 phosphatases regulator YPI1"
FT                   /id="PRO_0000333482"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   117 AA;  13089 MW;  CD9617822D63F381 CRC64;
     MAQQGSSQMR PQGTSSVTQT TTETSASPIL HLRPSKRKSK KKPSVRWTED TVDNEHMNKK
     KTKICCIFHP QRQFDDGSSC ESCSSSDSSS DGSDTEDSKP NAYEHQPHYK NQSKVPQ
 
 
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