ID A0A1B9GU86_9TREE Unreviewed; 1123 AA.
AC A0A1B9GU86;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=I316_03658 {ECO:0000313|EMBL:OCF34617.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF34617.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF34617.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF34617.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV700124; OCF34617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9GU86; -.
DR STRING; 1296120.A0A1B9GU86; -.
DR Proteomes; UP000092666; 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; 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 SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
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:UP000092666}.
FT DOMAIN 709..766
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 886..1048
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 966..1035
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 123969 MW; 2815F8138878175E CRC64;
MSRSRSTTPG PTGGRSSTPL SAPPTPVTPT HLLPAAMERA RSSEAVLGAG PNLAKTLIAE
REGRRREVKD TSLKREWENV DGYFPAPEIQ SDEEEDKMDI DGEESGPSTT QSPRSGTDQL
NHPETEHEHK QTVALGEPIE SSDQEVAVHL PTPPEEGKPY IWGMPKWGCE TERREVRKGV
RLVGMEELPA LVDRHSMLDT PSSVMFPWLH GISDDGQKGR DMAAFFGHAP PFEPPPYRGL
CLLFCPPHPL DEPRHPHRPK MPRTDTDQTT QQPSYEMPPP RERSETMSTS SESYHSSGTT
EATSPSIAGY SPLSSPGMDK LMPELETEDP HNEETEDVDV AMHPCDSKRV SPVAIASGLD
EPHHPMPCAE TSKIGSPIEE EVDSSDDSSE VDSEDQRPTC ILYNALHVTD VFDLPKHGDT
LKPPRFRQAK LPHQINLRNL NIQQIKYGTV SDIILYSKTG VGNGILEVAE QIARAQDELW
QIRMDEFYRH VGGSRPKGEG SSEPVKYGVW VVVEPFSKVE KHCPHLVNIT SKGENNHEAF
HTDLFEREAR ESRAMTRGSE VVEGLWVGND CDVPGGADDG AGAEVPFDLC LRASECADMP
SPAGLVKAYQ HLLQLDRRRR TVEERSSSWT ASPATIALRN LLSPSPTSPT TSDVPSKRLG
SPTPNDRKLR SRSEAPVADH EYVQLECSGS CRTITGQIRN PIYMTDKVVE LVYFLRKLVE
GRDKSGIKRR VLIHCQDGYT ESSIIVLSYI MSSLSCSLSE AFLHLQLVAK RSFFLYPSDK
PLLRRVDLKL AADRRAKAVK LVSNTAPHSS QPTESTGNGK SSPRWRGWGI PFSGSGSSPT
SAKGPATITT STVDVAKEML AEQDNGGSKV ALESKVWFED RRFDGFPSRI LPFLYLGNLE
HADNAAMLKA LGISHVVSVG ESLVSVPEHE NHSTTPGNSL CAHARAGQIS VLDLTDVRDD
GNDPLRPVIA RACAWIEQAR RDGGTVLVHC RVGVSRSASI VIAYLMQFER MGLMDAYMMC
RARRLNVLIQ PNLRFFHELF GWEVELARQE EETSRQQGTT AATAEDTEQQ GPDREEEDSL
LMAQFLSRPT LPQPTLPVQL RKDTGSRPIR SAAKELHPQG SAG
//
