ID A0A165G7H4_9BASI Unreviewed; 997 AA.
AC A0A165G7H4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=CALCODRAFT_469527 {ECO:0000313|EMBL:KZT57693.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT57693.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT57693.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT57693.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV423960; KZT57693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165G7H4; -.
DR STRING; 1353952.A0A165G7H4; -.
DR InParanoid; A0A165G7H4; -.
DR OrthoDB; 2045814at2759; -.
DR Proteomes; UP000076842; 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; 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:UP000076842}.
FT DOMAIN 786..961
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 883..948
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 109074 MW; 4B83B9EADDFC98D9 CRC64;
MSVSADNTDT LAPPPSKPSS PAPSLLAAIN PELPVEGVQY PPGFLDSLKL IHDRPGPFTP
IRAINADQLA QLRLIAATAD VPDAVLFPYL HGLDGDNEAQ NQFFAQQAMI ARGPSTAHTN
SFLIPHYRGL VCVAAEEHEK ESDWVDEDED SMMDDSDDDF YDEDDAMSDE ARGHETDNST
PPDADAVPSL DHSREASEES STSASSTPNT DSPPASVFGQ SLPSPASALE RNGQKLVPGS
ISRGATTTFQ SAITPLLTSS FRAADLLIDP TSDNAEFINP RIPDGISLRN FGIQVGKYVS
LADIVVYSAG GLTNAAINTA KRFKHAIERK AAERHQRWPD VPLVAYNVFV VTDPFNVIEQ
KYPHLVAIDS HGLSKNKVDF LAREKEEMRN LTRASEISPH VWLGNTMDAP MPFRATSADP
FDPTGNDGLY DICIECHEGV PFPTSSHVRQ AEEHLRNLDE RWSQHCVATG SPGRKRISSP
PLSPKSPVSP TTSAILELSE LHFTRSKSGP PTPLTLSGST SPSETPRVSR REPSLKPRPA
PNPMSAIHLL FPSSPPSTQN TLSQLMPFLE FLERAINPEW TPSSRYGSGR PSSAGSKTGQ
FRPSRPLKVL IYSADGYTES SFLALCWLMH HLELSLPEAY LDLQVEKHRS FFVYTNELGV
LRRIEGKMQE DRANDAASVV SAEQVAATIT TGPRELGVLT SGPGAAVGKK WRIGSQWRTR
SQSNAAAQPM SSLMSSSVPT TPLDAELSIV PKSKVSRRPR ASTSPSLPGF PDHQIWFDDP
RFDGSFPSRV LPFLYLGNLN HASNAYMLHA LGITHVVSVG ECALVPPVGH GENGTGFNLV
CPVTHSLAGR GSLWMEEREG RIKVLDIKGV CDDGIDSLRP QIRPIVEWID KARAEGGKVL
VHCRVGVSRS ATVTIAYVMK HLKCSLVEAY LMVRSRRLSV LIQPNMRLLY NLCGWEIELA
QDEIQASNAP ETYGMEQRLS WPYLAKEVHT LNERYLS
//
