ID A0A1Y2MFY7_EPING Unreviewed; 1182 AA.
AC A0A1Y2MFY7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=B5807_01220 {ECO:0000313|EMBL:OSS54407.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS54407.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS54407.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS54407.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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; KZ107838; OSS54407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2MFY7; -.
DR STRING; 105696.A0A1Y2MFY7; -.
DR InParanoid; A0A1Y2MFY7; -.
DR OMA; PNGPICI; -.
DR OrthoDB; 53899at2759; -.
DR Proteomes; UP000193240; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193240}.
FT DOMAIN 304..508
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 428..485
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 127896 MW; CFD395C8C18202A2 CRC64;
MPTTTSRKFM PMPSLGAVFG ADSHSIGHAH TADRDSSTAH GNNVARRTTS GTTTHGAPFS
SFHNHHDSRD SNSTTSSDNS PTTTISTMDS SSVTDPSPGP SPESPMPKIT NHSFAPDFRA
RRPETSDGVS SAHNFFELAR PTTPAKKARN LKNLGINTTT SLTNLRAQGP AAAPAPADTE
KNSSAPPSPL FIKPPTPPRR RPSNLSLTIA TPGINDNKPT RLVIPSTPSL SRPTLRHFQS
SPSLPLCSPS VAPTGGMKFP ALRPIVTKTS GLSEVPFEME EEEEEPNFDI PQSKEEKPAA
YPNGPICIYP AGVYLYFEPT PEQAASFDVI VNVASEVQNP FTSYSSESQK DLNKRRVDGP
AAENVDFAAL SQQPKTTFGF GNDSPTTPKA SAPVLRTIQP GETTINGKIY RTPEYIHMPW
EHNTDIVPDL YKLVKIMDDR VKQGKRVLVH CQCGVSRSAS LVVAYGLYKD PEVSVQEAYD
KAKKRSKWIG PNMNLIMQLQ EFRNGLIRQN QSNRTQNQGY GRRVGFPSSA NQNNRFSCPN
PGERDDVSGT RVPQTAPLPP DNDISMQRAS TGNMMAISPG PLSAPSGAFA ARFRNSWDSS
KSSLELSNNT TPSTTPYVDP KGHVIPVVEV QLNGSTAIPA TPEVISPALE LVPKASSVPN
FSRQLSLRSY QDAPAEQSVE TKSSFLAPMA PSGPAPLKSP SALTFNLPSF SMQEDMDDDY
EMKSPVKASF DLPWPSEYDE PAAPSLSVPK AQGSFQLGAP PKSPMFAPAM GFQLGAPPKS
PMFAPTQGFK LGAPPKSPMF APEGQGSFQL GAPPKSPMFA PPRMTLPKMR SDRSEKPRSL
LPFRAAEQTN EPVQSQTSLG APEASVPDRS PGFASPTFGS FPTDAFGPSS VPKSDMTSPR
GAEFHMAPFR PTVADDDPFG LTSPTRRDFS SGNQFNNRSS ASSIKSGSED RRPAFQAILP
PAHQTFNGFA SLDGHARTPS TQTLDQPPAP LQAPAPLQAS SPLQAPPPKR KPKFESHIDS
PDASPKSNRV ASMPTVSQAP PPPPRPETPR TQDFLATPAK TIRTRFSSPN MKEQRQLSKL
QTEMESKLAN RPERPQQAMD DLDALMSPRA EEFTRNPFHL DLTSPTEEVS PASSDETIKD
DKNGHTWSDP PRQWTPEKLT VDPRSPAQLG SSPIVRNIWD VL
//
