ID   YPI1_DEBHA              Reviewed;         135 AA.
AC   Q6BSZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Type 1 phosphatases regulator YPI1;
GN   Name=YPI1; OrderedLocusNames=DEHA2D04730g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382136; CAG86811.2; -; Genomic_DNA.
DR   RefSeq; XP_458672.2; XM_458672.1.
DR   AlphaFoldDB; Q6BSZ8; -.
DR   STRING; 4959.XP_458672.2; -.
DR   EnsemblFungi; CAG86811; CAG86811; DEHA2D04730g.
DR   GeneID; 2901253; -.
DR   KEGG; dha:DEHA2D04730g; -.
DR   VEuPathDB; FungiDB:DEHA2D04730g; -.
DR   eggNOG; KOG4102; Eukaryota.
DR   HOGENOM; CLU_098333_3_0_1; -.
DR   InParanoid; Q6BSZ8; -.
DR   OMA; HIQWAED; -.
DR   OrthoDB; 1599272at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
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..135
FT                   /note="Type 1 phosphatases regulator YPI1"
FT                   /id="PRO_0000333475"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  14892 MW;  16FD73BC4EAC2E0A CRC64;
     MSVNPSNNTT TSTETNTETR PILHLRNKKT DKTAKPRVRW TNDVVDNENM DKKKSKICCI
     FHPQREFGES SSESSDESSD ESDHSDDGAG EGASNGASNG GSGNDACCGN HKRKQKKPRK
     STPNAYEKQP TYKNK