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