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Database: UniProt
Entry: A5DLN0_PICGU
LinkDB: A5DLN0_PICGU
Original site: A5DLN0_PICGU 
ID   A5DLN0_PICGU            Unreviewed;       930 AA.
AC   A5DLN0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=PGUG_04181 {ECO:0000313|EMBL:EDK40083.2};
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 {ECO:0000313|EMBL:EDK40083.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK40083.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., 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., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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DR   EMBL; CH408159; EDK40083.2; -; Genomic_DNA.
DR   RefSeq; XP_001483452.1; XM_001483402.1.
DR   AlphaFoldDB; A5DLN0; -.
DR   STRING; 294746.A5DLN0; -.
DR   GeneID; 5125112; -.
DR   KEGG; pgu:PGUG_04181; -.
DR   VEuPathDB; FungiDB:PGUG_04181; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   HOGENOM; CLU_008439_1_0_1; -.
DR   InParanoid; A5DLN0; -.
DR   OMA; NKPYSRQ; -.
DR   OrthoDB; 2045814at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:GOC.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:InterPro.
DR   CDD; cd14516; DSP_fungal_PPS1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR047949; PPS1_DSP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR47550; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   PANTHER; PTHR47550:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE PPS1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT   DOMAIN          722..898
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          820..885
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  104869 MW;  D3D26C065B70CC4D CRC64;
     MDNGSSTLLS FPSSSEPPGS NVSSPPPAEV PRSIEEDSYV RGASKRSSSS SNDLLYERDR
     FRARLQTFNG RQNDKMDTED SPGTTESSKN GVIDEETSHC DVCDIIQSKT TRLQVRQPTP
     EFSNDNISPL SSDSVFFNSL SELPSSLSSS SFPMTIRSLT YAQLSAVFKY YFNQNLPQTE
     KMFPWLHGIH PDNFAQKRFF CRDTSDETDS GSEPPESNEL NPSLSPDATT APRFLMCVSP
     VDNPTLLRNT VHAPEILHPI DVSRAEVVRF LQYVLELVFP GKDQDHMLET IVADCYAIKH
     LPVFLNLDPS SGVSLRNFHI QVAKLAACSD MVIYCLDNEH LGSCKCASLA RVLWLAQRYT
     FAKDGALDKM HYNTFIMSDL PFLEKILLRQ SSPYHSTLFT VPPEPRNDTR KTSLESRLSS
     FNPKSLAVWD SDFVMKEKVE TTRMSAASCI GGRVWAGNMW DYQAMIMHLQ FRNEMSIGDG
     FGCYCSPSSS IVNKEDIANQ SITKILPPPR ANWRLFIHCC SDASFPDLAV LRSLMFKFSL
     SSHRSTGSEY HTLEFPPAGS VGIGDCKKEN LMSVVNCCKL LYLYSSSTSD DPDVVSALIY
     CSDGYTESSL FVLSYVMYSR NVSLDEAMLL LHNDYPRPFY IFSSDVHILR KLEVLLRRVS
     PLVKKVEWST LEVFSDLEIT EILLATGSRP SHSVGAKHSL ERKASSLSLL EADWVSDVDG
     SLPSRILPYL YLGSLKHANS LALLSKLGIT KVISVGERLE WLNSRHFQST HTISVEEIDN
     GNIEKFTISG NPSTVDTILK VNNLQDDGID ELSASLPRML DFIEAEHQKS NGKAKIFVHC
     RVGVSRSATV VMAEVMRRLN VSLAKAYLYV RVRRLNIIIQ PNLRFMYELF KWEEQQKFLK
     KNKSDLTLRE IDWFVFCREV MNLNVPYLRK
//
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