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Database: UniProt
Entry: A0A371CUX8_9APHY
LinkDB: A0A371CUX8_9APHY
Original site: A0A371CUX8_9APHY 
ID   A0A371CUX8_9APHY        Unreviewed;       790 AA.
AC   A0A371CUX8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=OH76DRAFT_1409452 {ECO:0000313|EMBL:RDX44088.1};
OS   Polyporus brumalis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX44088.1, ECO:0000313|Proteomes:UP000256964};
RN   [1] {ECO:0000313|EMBL:RDX44088.1, ECO:0000313|Proteomes:UP000256964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX44088.1,
RC   ECO:0000313|Proteomes:UP000256964};
RX   PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA   Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA   Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA   Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA   Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT   "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT   exposes the biotechnological potential of its oxidative enzymes for
RT   delignifying raw plant biomass.";
RL   Biotechnol. Biofuels 11:201-201(2018).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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DR   EMBL; KZ857455; RDX44088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371CUX8; -.
DR   STRING; 139420.A0A371CUX8; -.
DR   Proteomes; UP000256964; 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   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF519; DUAL SPECIFICITY PROTEIN PHOSPHATASE MPK3; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT   DOMAIN          519..668
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          585..649
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  86028 MW;  94FEED9CE25FDB24 CRC64;
     MPPSKGRPPN LRLHTNAAKT PSNTIIELET PVDRADDDDD LLQLSSPSTA SSSPVEYASA
     VESDSDPTSD DISKELALLD RLRRSVRKNL KLRPIRSATN IRAQAASPFS SSWTDLREAR
     SPSPSSSAAS PASVYYTPTS ALYADVDDWR SSSSDSSVTH GIDAAVLVAR LAAPTRPILI
     DTRPTADYLA NHLEHSVNIH TIPSLILKRS RKPGGGLHDV SALRQWITTD DGKRKWDDIM
     NSGDWDGDVI VYAEHMDEKD RTNPQATAWI LLKLVEPLLE HGTIDYLHGG FSTALRHPYL
     KQRIVSDRSR QDSHRRPPTK AQKVNGKPGG LFQLDISVAT RPRDLPELER SAVSPKPMMP
     TAITSWQDTS DPVAPSPAPS QLGFTRPPPP RRPSVPTLRK LDTTSTERLN ANLPKLQMPH
     KSATLAAPPS ASGLRSRSRS PSHLRLDLPP LSPPGSARLL SASPGHSSEF LPPPSPSWAQ
     PSTPRMMHSP STPMSRSPST ARPESSQPPT TEEPFPAFAA STILPNFLFL GPEVTAEEHV
     EELLSLGVKR ILNLAAECDD DQGLHLRERF ERYIRIPMRD TVEEDNITRG VREVCEILDD
     ARLHSAPTYV HCKAGKSRSV TAVMAYLIHA NHWTLSRAYS FVLERRKGIS PNIGFVSELM
     TFEEQELGGK SVGVVKVSEG EEGEGDGGGA GGGGGGSNYQ VALGSRRPQH IRESLPPLFS
     MPHSFAGISS STSNGPPVLD AAHIGDSGQE LEIKDATGRY RHARRAPVDE ATLQPMRRVS
     KAGLESSSYV
//
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