ID   PTPX_CANAW              Reviewed;         597 AA.
AC   P43078; C4YD44;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable tyrosine-protein phosphatase;
DE            EC=3.1.3.48;
GN   Name=CPP1; ORFNames=CAWG_00432;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WO-1;
RA   Csank C., Dignard D., Thomas D.Y., Whiteway M.;
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; L01038; AAC05307.1; -; Genomic_DNA.
DR   EMBL; CH672346; EEQ42230.1; -; Genomic_DNA.
DR   PIR; S43743; S43743.
DR   AlphaFoldDB; P43078; -.
DR   SMR; P43078; -.
DR   STRING; 5476.P43078; -.
DR   EnsemblFungi; EEQ42230; EEQ42230; CAWG_00432.
DR   VEuPathDB; FungiDB:CAWG_00432; -.
DR   HOGENOM; CLU_032220_0_0_1; -.
DR   OMA; INYSPKH; -.
DR   PHI-base; PHI:66; -.
DR   PHI-base; PHI:6828; -.
DR   Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase.
FT   CHAIN           1..597
FT                   /note="Probable tyrosine-protein phosphatase"
FT                   /id="PRO_0000094918"
FT   DOMAIN          428..579
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          55..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        516
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   CONFLICT        504
FT                   /note="Q -> K (in Ref. 1; AAC05307)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   597 AA;  65586 MW;  B0F1DE22ACC9C78C CRC64;
     MTTPLSSYST TVTNHHPTFS FESLNSISSN NSTRNNQSNS VNSLLYFNSS GSSMVSSSSD
     AAPTSISTTT TSTTSMTDAS ANADNQQVYT ITEEDSINDI NRKEQNSFSI QPNQTPTMLP
     TSSYTLQRPP GLHEYTSSIS SISSTSSNST SAPVSPALIN YSPKHSRKPN SLNLNRNMKN
     LSLNLHDSTN GYTSPLPKST NSNQPRGNFI MDSPSKKSTP VNRIGNNNGN DYINATLLQT
     PSITQTPTMP PPLSLAQGPP SSVGSESVYK FPLISNACLN YSAGDSDSEV ESISMKQAAK
     NTIIPPMAPP FALQSKSSPL STPPRLHSPL GVDRGLPISM SPIQSSLNQK FNNITLQTPL
     NSSFSINNDE ATNFNNKNNK NNNNNSTATT TITNTILSTP QNVRYNSKKF HPPEELQEST
     SINAYPNGPK NVLNNLIYLY SDPAQGKIDI NKFDLVINVA KECDNMSLQY MNQVPNQREY
     VYIPWSHNSN ISKDLFQITN KIDQFFTNGR KILIHCQCGV SRSACVVVAF YMKKFQLGVN
     EAYELLKNGD QKYIDACDRI CPNMNLIFEL MEFGDKLNNN EISTQQLLMN SPPTINL