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Database: UniProt
Entry: A0A0G2H6Y9_9PEZI
LinkDB: A0A0G2H6Y9_9PEZI
Original site: A0A0G2H6Y9_9PEZI 
ID   A0A0G2H6Y9_9PEZI        Unreviewed;       646 AA.
AC   A0A0G2H6Y9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Protein-tyrosine phosphatase 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UCDDA912_g09116 {ECO:0000313|EMBL:KKY30938.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY30938.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY30938.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY30938.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY30938.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY30938.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY30938.1}.
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DR   EMBL; LCUC01000431; KKY30938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2H6Y9; -.
DR   STRING; 1214573.A0A0G2H6Y9; -.
DR   OrthoDB; 1342035at2759; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; 2.
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:UP000034680}.
FT   DOMAIN          181..585
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          446..508
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  71810 MW;  6DE30E57E3976102 CRC64;
     MDRLRSGFHR KSRKASPSRP TVITDGTHSA GKTTPEPVSA SSPLQVPHLP NKEKKTSPFR
     SLRDFSRSHK RARSPAAGSL PRSPIGATYT FDGLDETPTT SPTVRGGSGD LHPLQQEMSG
     DPTGVPPPKM PSFLSLPAQD IVAKFQEIVW MERNRIMQSL TNPSPDFKWA RVTGDHLKKL
     DRYMNIQPWE NNRVRLRVPP GRVDYVNASP ITLSSTTPQK ASRTQARGSS NKEAAIVGLS
     DLAGGGPDRY IAMQGPKRNT TDHVWRMVVE QLESPAVIVM LTETHEANME KCYPYFPRSP
     DDAPLEINER DEFGDAFRAS VHCEAIEETE AGDAIELRKL VVRSYKSPSK ATKTRSGGDR
     DNLTTPVSAV DGSGDVKMLS PLKTAPDNED LSQEDGSDDK SINAELGESA NTHQKELPGE
     YEERVVWHFL YKKWPDFGVP ALEDLDSFFT LMRLSREKNA SPENPRIVHC SAGVGRSGTF
     IALEHLMREL DAGVLDHWDS PSHFRHRRTD GGELAAAEGD NNNVHHRSDD DSDGKMDVED
     QHTTTTDVEG DDLIFHTVNQ LRVQRRSMVQ AEPQFLFIYE VMRKLWEDRY GSDGSPSSTA
     AAQRSTPPPR INGPGDAGGE DSDIGQPARK RQEFDPFIEQ QRDHQA
//
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