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Database: UniProt
Entry: A0A0H2RWZ1_9AGAM
LinkDB: A0A0H2RWZ1_9AGAM
Original site: A0A0H2RWZ1_9AGAM 
ID   A0A0H2RWZ1_9AGAM        Unreviewed;       721 AA.
AC   A0A0H2RWZ1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=SCHPADRAFT_889620 {ECO:0000313|EMBL:KLO13928.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO13928.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO13928.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO13928.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ085951; KLO13928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2RWZ1; -.
DR   STRING; 27342.A0A0H2RWZ1; -.
DR   InParanoid; A0A0H2RWZ1; -.
DR   OrthoDB; 53899at2759; -.
DR   Proteomes; UP000053477; Unassembled WGS sequence.
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   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:UP000053477}.
FT   DOMAIN          167..360
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          266..334
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..635
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        50..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..600
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   721 AA;  77463 MW;  5AEC1B9BFB1FD18D CRC64;
     MQHPTPADDH TQTPRPVSAF QQSRRKGPPA ALRIHAPVQN PPIAIMLDDA TSTASASSSN
     ASSAASDSDS VLLPFTRPDK PRSMRNMKRL SLVLPSALDN RSSNSLPLAS DPDTTITPSD
     DASQPSSSSS NACRRRPSVI SLPPSRGATR LHRKDEDESP TIPYLDGPVQ ILPGIWLGSE
     DNARDWDTLL KRGIRSILNV AREVNSPFDS NATTQPLRPF VSEPDLKEKS RESQSTFHPA
     HAPTGRPAMH YLKLPWSHGQ KNLVHEGFVD AMAFVDAALE RGDGVLVHCQ CGVSRSATVV
     IALVMRAAAL ELPSVSPDVW SLKSGGMHAA YAYVKEKSKW AGPNMSLIYQ LLDYERVLNG
     ADKSPSASEN SSAAAEDDEE WSRRRRLMEE ESSSADADND REIAEVMREA HALDKAMEER
     VVSRKASGSS LGSSTGIGMG SAWKSRYRAG SVTSNFTSGS ILDENLIEEG EEQELLGVGG
     GFDAPSLSIR SPSGETTESS EANSSSPDWK NEPGTSSFLL DVPPPPTARP EMLGKQRSFT
     DSDIQSKLRP PPSAPPTKST FGFTSRFSFK LSLSKRQPSA LPPVPSSPIV SAPPEDPSPL
     QKGLPSRKRI PPPLRLHSAT QSRSSSRSSQ LSKLSTMSTP AQTLFVFPPS PTLQSHTPSM
     VTVTSNLGAP SPFGPAIPTP RVSTFKNDGR RRSFIGLGAP PTPTTACSRV DARGWVSLGP
     T
//
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