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Database: UniProt
Entry: A0A165LKI2_9APHY
LinkDB: A0A165LKI2_9APHY
Original site: A0A165LKI2_9APHY 
ID   A0A165LKI2_9APHY        Unreviewed;       591 AA.
AC   A0A165LKI2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=DAEQUDRAFT_732477 {ECO:0000313|EMBL:KZT64540.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT64540.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT64540.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT64540.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV429125; KZT64540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165LKI2; -.
DR   STRING; 1314783.A0A165LKI2; -.
DR   OrthoDB; 5472710at2759; -.
DR   Proteomes; UP000076727; 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; IPR003595; Tyr_Pase_cat.
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   SMART; SM00404; PTPc_motif; 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:UP000076727}.
FT   DOMAIN          1..140
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          61..121
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          213..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..372
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63393 MW;  135340266B9696EE CRC64;
     MDEVIPGLWI GDLSSALNTE QLREHNIRSV LTAMRGRVRI DETFNNLQIN LDDTEDADVL
     GHVVTAIQFI ESELEKGRGV LVHCQAGLSR SATIVAAYLM YVQHIDYEAA LDLIRDVRPN
     VQPNEGFLRQ LAVFQEASFR VSRRDKATRM YYLERVVEEV MNGDGTVETE FFAKFPRTPT
     DSAPATPGAG PRRRIRCKMC RQELAAREHM LDHGQVGPDT PAFASPAVSR RPSSSLYDAS
     ARPFAPLTAA KSPPGSRRQS INDMRPTISS PLSPTGSRRP SMNDTIKPVG LMPLTPIIAP
     GSVPMSRRPS ASARESMTRP RLGSSADTRP LKSSLLALED AAQLGRDISD ELSESALDGS
     DDEDDEEEDE EVRNPPNTAL PRVTEDADSA SLSTASSPTA VSTPGSRDLS MKSLSLKGAM
     PSPPVRSAPA SASCGEPLPA IPPALVRRIS SSSGSSFAHG SDLAAQLSNN PKLAALRSPT
     NGLDMMVITP PSAAAGSSGP GSGTIGRGGS AFSMSPPLLA NNTCSGYFVE PMKWMDFFLQ
     DGQMAGKIIC PNKKCGAKLG NYDWAGVCCS CKQWVVPGFC IHRSKVDEVV V
//
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