ID W9Z263_9EURO Unreviewed; 562 AA.
AC W9Z263;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Protein-tyrosine phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O1_01166 {ECO:0000313|EMBL:EXJ96040.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ96040.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ96040.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ96040.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ96040.1}.
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DR EMBL; AMWN01000001; EXJ96040.1; -; Genomic_DNA.
DR RefSeq; XP_007720269.1; XM_007722079.1.
DR AlphaFoldDB; W9Z263; -.
DR STRING; 1182541.W9Z263; -.
DR GeneID; 19156068; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_001645_9_12_1; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000019484; Unassembled WGS sequence.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd18533; PTP_fungal; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
DR Pfam; PF00102; Y_phosphatase; 3.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 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; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT DOMAIN 67..449
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 328..440
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 62079 MW; B4E8818E0FBFCB50 CRC64;
MPQSLIISTP PSHSVKRQRS QEIGPESSRP ASSGTTPSTR STNEIDDSAR QVALKLPSYL
KKTRQEITTA FQDLEWKQRY RLQHAFQNPE TSPFRVDRSP AVVSRNRYGN VQPWESARVK
LRKPIGGSDY VNASPITLSS RNVHQYQRSD SSASASAAQV ECRYIASQGP KEGQFSHFWH
MVMQETTGEV GVIVMLTQLY EGNKEKCAQY YPPNFDNPTI ALAAHEDGNG NESARSTDDG
DPFLDAPAMI ADADGVGTDS HSDNPASQSD QANQGQCGTV TLMSLHEDIK LGCEVRRLKL
TIDGESKEIY HYFYKNWPDF GKPEAEDRKA LMELTKVTKE VAGDSPRVVH CSAGVGRTGT
WIALDFLLQE LEAGVLIESS SYFANHQPPS RSSSNATWGK SGPSKPTTPD SKDEEDAIFE
TVNALREQRM MMVMNELQYS FLYEALKEAF IEKYAQKETG PMVAGVLEPS PKIARKGAPF
GGMFEDTHVG QVQGDEDTVS EAGLESEAET EIMEKGKQDG DPQSALEAAT DAPDPYAAVA
PETIREGQRK QEQDEVRDHE VK
//
