ID G0W9G2_NAUDC Unreviewed; 530 AA.
AC G0W9G2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=NDAI0D01100 {ECO:0000313|EMBL:CCD24423.1};
GN OrderedLocusNames=NDAI_0D01100 {ECO:0000313|EMBL:CCD24423.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24423.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD24423.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR EMBL; HE580270; CCD24423.1; -; Genomic_DNA.
DR RefSeq; XP_003669666.1; XM_003669618.1.
DR AlphaFoldDB; G0W9G2; -.
DR STRING; 1071378.G0W9G2; -.
DR GeneID; 11495233; -.
DR KEGG; ndi:NDAI_0D01100; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_036115_0_0_1; -.
DR OMA; HIEWTHT; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000000689; Chromosome 4.
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 CDD; cd14521; DSP_fungal_SDP1-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF531; DUAL-SPECIFICITY PROTEIN PHOSPHATASE SDP1-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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 {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 226..366
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 287..342
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 59105 MW; 7F53DD6E514B2B35 CRC64;
MAERRDSFVS RSMKINSKSP RSLQSRNTKN LSLSFQNDEF MKPLKVAPAS SINQAVSVSA
ASLTAPLIIN KNFVSMKQQQ QQRPRLFNRS SEAAIYTLPN SSRPINPGPL SLSINKNKID
DDANNNSNND NFSNNIPKST NEGGSVAPPI PLSICTKKSK SILKRSKTLP SLETSTPLMQ
DRNSNSNNTQ TTFIFSDKGK DVNSINGQYL QTDYHNVFKK NAYPDGPLLV IRPNIYLYSE
PRLEEILSFD LVINVAEEID NLSTHLPTNK NIEYYQILWS HNSKISEDLK ELTEIMYHAT
LQNRRILIHC QCGVSRSASL IVAYIMRYHH LNLNKAYDEL KSIAHDISPN MGLIFQLMEW
NEQLTRMNEA ATENLQNNSS GITHSTISND FDEQASSLLD ADVTSSKNDN NNNNNNVSDT
SACTASSASS SSSASSSSTF ASSNLITTTT KMETIVSESS LSTMFNYHDP EDESIIDSEN
NNINDGSSQQ QQQQRSSFIN SSSKYTPFFS YIALNNILPQ LINLSKNSIH
//
