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Database: UniProt
Entry: A0A0F4GAZ9_9PEZI
LinkDB: A0A0F4GAZ9_9PEZI
Original site: A0A0F4GAZ9_9PEZI 
ID   A0A0F4GAZ9_9PEZI        Unreviewed;       816 AA.
AC   A0A0F4GAZ9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, 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=TI39_contig4184g00003 {ECO:0000313|EMBL:KJX94509.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX94509.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX94509.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX94509.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-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}.
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:KJX94509.1}.
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DR   EMBL; LAFY01004143; KJX94509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GAZ9; -.
DR   STRING; 1047168.A0A0F4GAZ9; -.
DR   OrthoDB; 53899at2759; -.
DR   Proteomes; UP000033647; 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:UP000033647}.
FT   DOMAIN          320..470
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          390..447
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  88498 MW;  8EF10DD6F24A3678 CRC64;
     MCSSFTSPAN MSPTEGQTKP LPHPSREGSQ TTLLPSSDYD HIYHKFHQHT LSDSTNTLGS
     NDSSPTTTIS TVDDSSATEP SPGSSPESPP PSTFAVGMLR PRTEDARSAP FFELQKQPPP
     RKGRNLKNLA VVTSRLNTRA SSTTSLPLRA AMEDSSLSPA FVKPPTPPRR KPSALGLTIM
     TPALGKPKPQ EVRLLIPETP SFGRPTLRHF QSSPSLPLAP GLGLPLSRDA KQRRNMETIF
     SPSEAKAPEV EIQEEEEEEQ NFDIPLSMED KPEAYPDGPI CVYDPRIDLY LEPTAEQARQ
     YDVVMNVASE VRNPLVKHDV PTPVEPDLRL DGGGGIQYAP KRDRPVSRKD EASPTTPKAT
     PPVAAFPADS QAKEPEYIHI PWEHNSDIVP DLLRLVKLID ERVMEGKRIL VHCQCGVSRS
     ASLVVAYGIY KNPDASVQEA YDAVKKRSKW IGPNMNLIMQ LQEFRSSLAR GGLLGDRTLS
     PRTPSSALSE WKGPFSDRAT PMSGKNMTIP DAEVNASSGP AADEAPISPG PSSAPSGVPW
     QTGVPSRTRA LSAVKPATAY VDPSGNVIVP VLKVLNINSP RIDTFPQPHS QSDPQLPQLQ
     SPTSTQFATP PSHSSIHSPT SESFNLQSPT STSFPSSISI NDDDDTHPFT RASLLASIGM
     ASTRSTDEEE PPRRRSSSRQ PTAAVGRMRS RSNLSPTTAT TAPRRLAVKI SSPNLREQRQ
     LQEMQGRIER ELASSRSGSG RGGKEEDEEV ATSPRVGEFL ANPFKLGFAI PSTSETERAE
     SNGSSPSGLS ADDPRSPVGE RMKGVNPFRR NIEDVL
//
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