ID A0A2A9NCZ0_9AGAR Unreviewed; 1630 AA.
AC A0A2A9NCZ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-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=AMATHDRAFT_8867 {ECO:0000313|EMBL:PFH45646.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH45646.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH45646.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH45646.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ302320; PFH45646.1; -; Genomic_DNA.
DR STRING; 703135.A0A2A9NCZ0; -.
DR OrthoDB; 2045814at2759; -.
DR Proteomes; UP000242287; 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; 1.
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; 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:UP000242287}.
FT DOMAIN 1393..1580
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 1491..1567
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 154..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 175419 MW; A49EF76D4795427F CRC64;
MLHPGRHRQQ IEIHGLDYNT AFLDALPVVP NKHFQTSTVT TTTTTTTTTT TSNPIRLLSA
KQFSDLHLKH ILAHPQDHVL FPFLHGLEGD NHAQNAFFHS SAIGAPTKSY GSPATVNPHY
AAKVPRYRGL VWVVCEDDLQ LDGNEIALCV LRRKPASESS EGESEESVGS SGSSFGDDDD
EDDDTDSEEE PREMAMLVKD PPAQTITTTT TTTASAIPMD LDQHNDHDHP DDNNTPDIPV
DSKDKSPDEL PHMHPVQHRP TIQTTNLPIF HPNPVPAAVA STTTATTTSA TDPSSTSTSS
TSSESSVSSG ASFFALGSSP VSTATSLDSE SCSPLDVGPI SAQDPTPKPS TDPTETAMIA
DPPLDVPIPA ATQPQAKPKP ACFSPPLLTS TFRPKELLRR CAPNTKQNQG SKKTTRKEHH
HHHHQHHRQE RARTSSFAPG PVPPSTSTTS SPSGGENEWE FVPAQVPEGI SLRNFGIQVP
IYATLSDVVV YSPKGPTRRA LALAERFRAA IEKKRRERIE KRRAARLALQ QEKDQQPQNG
ARPVILTLPS FHGGSNEGGN DTTTSTLPSS EQLQQTIVED EEALLHYNVF VLSANEEEMR
REIPHLMMRI SIDPELSASA GWESGDNPLD VSSSSSSSLP SASSGVIVGI GGTGSNTTTI
HLGGGAHTDR SDGHVVEQVG MDVDEGVDVG AAGMGMEVDV DAAASTMMTT GASVRYSGVL
SKRNGGGGGG GGSFADDDIP NTVDFAQREK DEMRDLTRAS EIITCFPPSG PEEESMGIGV
GGRRGGARTK RNMGLGQPQP QQPPQYRDLS GTRTATHWNP NVGQVFLGNA HDVPLVLEAP
VRLAPVPQAS TYKEHQHHAA DQKMVIDDDE EEVGAKKRHG RRKGQPFARE EVVNEDDPLY
YQATNNPALG MGYDICVECH DLAPFPSAAH LRAAEEHLVA LEKLWADRCR DGMIQRRLQQ
QQGRGRYASP PPPLGGGDQE VIVPPRPPPN ANAVVHVPFP SSPPNGQATM ASLMPVMRFL
EKWVKPVLVP PTMTLPDYPP HQEEGAGGMS SARRWSTVGG NVSLFTGNSG GHGSRTRSFT
TSHAPSSTTT TSQQQQQQDT RSRPLKVLIY SSDGYTESSV PALCLVMALR GLTLPEAYLE
LQVVKRRSFF VYQADLGILK RVESRLLEER ERERLARVAR EREQRRQQQQ QQQVEGAEVG
NGNGNGNGNG NGNGAVNGRG DQSGWGGLSW FINEGYKQGG NDVGGRGSGT YYQQQQQQQQ
SSYPQQSQQS YSYHHGGGRP AAKSVSFARS PVVVGGQQQQ SVVSGQEGLT GVVGNGAGTS
GGGSGAASVP ATPSQGFVSV AGQISGAAGP GERDDSVLSG RVGRPRANTS PWLPSLIGDH
QSWFNDPRFD GSFPSRVLPF LYLGNLNHAL NAYMLHALGI THVVSVGECA LVPPHGSGSQ
GYMRGAGNGS NGNGGGGGHY IAGKGPGGQG SLWIEEREGR IKVLDIKGVC DDGIDTLEPQ
LEPICDWIDR GRLEGGKVLV HCRVGVSRSA TVTIAYVMKH LGISLVDAYL IVRSRRLSVL
IQPNMRLLYN LCGWEIKLAR DRAARRGGEG DVGMEEQQDQ EEGLRRELAR TLSWPYLAKE
VHALNEKYLH
//
