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Database: UniProt
Entry: K1W6S4_TRIAC
LinkDB: K1W6S4_TRIAC
Original site: K1W6S4_TRIAC 
ID   K1W6S4_TRIAC            Unreviewed;       667 AA.
AC   K1W6S4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=A1Q2_08210 {ECO:0000313|EMBL:EKC97473.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC97473.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC97473.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC97473.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKC97473.1}.
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DR   EMBL; AMBO01000410; EKC97473.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1W6S4; -.
DR   STRING; 1220162.K1W6S4; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   HOGENOM; CLU_023312_4_0_1; -.
DR   InParanoid; K1W6S4; -.
DR   OMA; CCGCKEW; -.
DR   OrthoDB; 5472710at2759; -.
DR   Proteomes; UP000006757; 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   CDD; cd14498; DSP; 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; PTHR45848:SF4; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12; 1.
DR   PANTHER; PTHR45848; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12 FAMILY MEMBER; 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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          117..278
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          200..257
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  72376 MW;  6C3638838C15D146 CRC64;
     MTAQTAHATP KRALSRRPSL PERTKMTMTD LPPADAQKPD SLAVDDVFDQ LKATGSLEAA
     ARRLAEIAMR EETLPKVVQR RQAWEDDPEE AEWQQQQAEE AQGGAARRGE EEEEIEHLQQ
     VCDGLWVGDL VAAMDGEGLR ERGISNVVSL LRPRLNFDPE FAAYTIEIDD AQDTDILQFL
     PSTSAWIRDA LLKRQGTPDE ERDPAIEPRA PETNPGGVLV HCQAGMSRSA TVAAAFLMNE
     LELDPEDAVQ VVRDARPVVD PSETFWHQLG IYHQAKKRVT MKDRTTRQFY LERNAGMVLN
     LGGRPSMDHM AKYPLSPTAS TPQTPAGATG RRKIRCKMCR RNLATREHMM DHILAQSGGP
     ATRPATPSAF ALPQPLTTTE DATFQPLERS NSVSSVINPL TGLPGARSRR ASNASSRRPS
     LGAMSAISDG TTRSRSRSVL GNDGQLTMSR RDSSGSATGP SGLAPMTSPE AVKSEGGRPP
     TPPLPSDSKK EEKEPKEHKE EKKEEKKGPG GRPMLDADAL AARLPPQLAA LRAGFSATSN
     LSSPIASSPP SSPESELPPA RRRPSNLGMT SMPQPLTPAA LSALTQAHAQ QAAQNGPPIL
     TNNKCSGYFV EPLTWMEPAL NGQVSGKLFC PCGAKIGTFD WAGVQCGCKE WVTPGFCIHR
     SRVDEVW
//
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