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Database: UniProt
Entry: A0A3F3Q6T0_9EURO
LinkDB: A0A3F3Q6T0_9EURO
Original site: A0A3F3Q6T0_9EURO 
ID   A0A3F3Q6T0_9EURO        Unreviewed;       678 AA.
AC   A0A3F3Q6T0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=BDQ94DRAFT_16350 {ECO:0000313|EMBL:RDH34881.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH34881.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH34881.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH34881.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ852042; RDH34881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3Q6T0; -.
DR   STRING; 1341132.A0A3F3Q6T0; -.
DR   OrthoDB; 2045814at2759; -.
DR   Proteomes; UP000253729; 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; 2.
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:UP000253729}.
FT   DOMAIN          501..649
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          568..636
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  75667 MW;  45621517D9D0F0FF CRC64;
     MATVVVQQQT LRHSTPPPTG LTPALSLNRT SSPIPNKHIP VCPTGPSPIN AHAPSPPVKD
     SSNDQTSSLL YPPDKSRRLT HSPTVYTIDL KTLSASLEHL AAQPLPHPNL VFPWLHGLHP
     DNHLQVGFFT KGKRSLRRTP KCWRGITIVK VGGDLSSCRI KGAVSPEEVL APSGVEFLAI
     DPREGLSVRN FQIQTAKLAP LSDIIVYGEN SATQQQILDI ARRMATAQHN WRIKNDPDRN
     SPAYNTFVLD CAFSEVEKKA SHLVAISSSG QLTGQVVDFF QWERLEMCEM SKASEISTNV
     WLGPTPDYLL RPGSCGPAPT ENFDLLIEAS ELASIPGPRF LANLNKQLEE GPQKLEFPSS
     GSILLPSGET REIDDLVNTV RWIYYLANPD EPDQKADADG DIPMIPLTKT ARKILIHCPD
     GYTESSLLAI AYLMFAEGIS APNAWLRLHC EKKRNFFAYP SDITFMSGVQ RRLLQESPAT
     RSHKIRSLPD PAWFRYCDGS LPSRILPYMY LGNLSHANNP EMLSALGIKR ILSIGETVSW
     SSTSAKVDEK DILHITNVQD NGIDELTKEF DRCLDFIRQG KHDGMATLVH CRVGVSRSAT
     ICIAEVMASL GLSFPRAYCF VRARRLNVII QPHLRFVYEL LKWEELQLQK RNKPARRELE
     WATVAREIAL MNKPYSRQ
//
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