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
//