ID A0A0D2EHX0_9EURO Unreviewed; 820 AA.
AC A0A0D2EHX0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=PV04_02023 {ECO:0000313|EMBL:KIW73947.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW73947.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW73947.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW73947.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846956; KIW73947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2EHX0; -.
DR STRING; 5601.A0A0D2EHX0; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000054266; 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; cd14521; DSP_fungal_SDP1-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF531; DUAL-SPECIFICITY PROTEIN PHOSPHATASE SDP1-RELATED; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 381..562
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 482..539
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 113..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 89135 MW; B2C33A2F8ADA20C9 CRC64;
MDCLTDRHQR KRSFDLANDY QDITSTIRRC VRHASTPSAS SIACLESCQF TAPVTKRRPP
LYPTKYSNMP QVEIGSVMST PFPSFMSVVG KPESSLLKDM EELAAATGSI PDSDTQFLVT
DANPPSEAPI RRSALSLHHR DSVTSITSTS TDSSPTNTNS TFDSPVITDS SPGSSPESAS
SNAPVSPFRN IMIKPSIEPP RNPPPQSIPP PREEPSKPGL IPDAPKNVKN LSLNMGAVVL
SRPATSHGFE SHAFSAPTSP SKDAPRTGRK KPTNLTIRTP GFQQLTFNRA LDVPPTPSFR
PTLHHMASSP ALASLASPKK QPPGGLFLHL PASGIVISGQ GSDSSSSGNS ANGQLPELKE
EDEIHRPQKS QETQEKGYPK GPVLIYDSGV YLYLEPTAEE ASKFDTVINV AKEIKNPFRE
ASKPEILEPQ TAISELSFKS AWEWPQSSEV PTPSTPRPSS VGQKNPPEYL HVPWDHNSEI
LEDLYCLCRL IDERIQEGKR VLIHCQLGVS RSASLVIAYG LYKGYQPDFH SMYMAVKQRS
QWVGPNMSLI YQLTDFRAKV VKDVYGDHCN NPKESWWQIR PPSSPVMDTP IAKQSSWRVP
TGSDGRAPVS QSAYIAPPLA KAAPPLRLNK ELPPVPLFPR NEPTAVATPI KLSQILGGIA
RSSPEPATTP DPALAAETPS PPRTQSPPQS VSPRPLPFRE RFDAPPSQSM PNPSKTPRLG
LVTSSPRMDL AMEEPSSPSL FSPRAAEFMA SPFGITAAGD VAATQKLMKK PSKGVLLPPQ
IRPSVHLAAP GDQIPAPFDP RSPHQQGEGP EIFRNIEDFL
//
