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YPI1_ASPFC
ID   YPI1_ASPFC              Reviewed;         182 AA.
AC   B0XPZ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Type 1 phosphatases regulator ypi1;
GN   Name=ypi1; ORFNames=AFUB_008140;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP56113.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XPZ9; -.
DR   EnsemblFungi; EDP56113; EDP56113; AFUB_008140.
DR   VEuPathDB; FungiDB:AFUB_008140; -.
DR   HOGENOM; CLU_098333_0_0_1; -.
DR   PhylomeDB; B0XPZ9; -.
DR   Proteomes; UP000001699; 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.
FT   CHAIN           1..182
FT                   /note="Type 1 phosphatases regulator ypi1"
FT                   /id="PRO_0000333467"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   182 AA;  20048 MW;  A20155ECBB5DBA8A CRC64;
     MSRTRQVPSN TASSSHIQLL SPAVPQENHS TVRISGTLRL RAENDSIATD HIEGARPGRH
     IRWTEDVVDN EGLGKKSSKV CCIYHKPRPV GESSSESDDS TSSSSEPESD NDVDCRDSTG
     RAESHEQNAQ DASQSPSNRS LNRGRTPSYT KRHAKRNGKR KPSPNAYEKM PKVKGQPRKT
     GM
 
 
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