ID G2X9V9_VERDV Unreviewed; 953 AA.
AC G2X9V9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Tyrosine-protein phosphatase non-receptor {ECO:0000313|EMBL:EGY15990.1};
GN ORFNames=VDAG_07154 {ECO:0000313|EMBL:EGY15990.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY15990.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS572709; EGY15990.1; -; Genomic_DNA.
DR RefSeq; XP_009654354.1; XM_009656059.1.
DR AlphaFoldDB; G2X9V9; -.
DR STRING; 498257.G2X9V9; -.
DR EnsemblFungi; EGY15990; EGY15990; VDAG_07154.
DR GeneID; 20708617; -.
DR KEGG; vda:VDAG_07154; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_001645_11_0_1; -.
DR InParanoid; G2X9V9; -.
DR OMA; WQQDVRV; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000001611; Chromosome 5.
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 Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
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:SF532; TYROSINE PHOSPHATASE (PYP1), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G04710)-RELATED; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 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:UP000001611}.
FT DOMAIN 289..405
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 539..922
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 777..825
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 104217 MW; 73F80AC62056BEF6 CRC64;
MTESKTGERT PVHYAMKTPS TTRPSGAPRS SHGRAHSRSN SHAKRSSHGS KASTPVASPR
MPFSVGQAYP PPPRLSPGRI ADVRATSPNY FGWRPAESSN DGRTAHSCLA ITGAPLPLRF
FNLSSSHFGA PSTPGDAGPA AAPARPRPPP RWHTHASDSI SETPASRTTR ERPASRMDVD
QASSHDSAYV SSDSRPDVES SVQPASILGM PRSESPRQSA SSFERRTMLS SVEDRHPRLS
IPNSRPDPPT PSVLGRSHQR AETLPADMEH GPSLISPSHL KSLLESQTRD TDLLLLDLRV
SQQYLHARVK SALNLCTPTT LLKRPTFNLT KLQQTFQNPE DKEQFTKWAS TQNLVVYDSH
SSEKRDAMSC VNMVKKFVAE GYQGGMFILR GGFKAFSEAY PDFVETGAPT GTNCGSGPLG
NNSSGNAGIL PVIGGVMLPN ASNNPNPFFS NIRQNMDLAD GVGQLEIARP KGLDSPTLPR
WLRDASTLGD HGQQVSDKFL HIEKDEQSRM KKAYSVFNPE SKSMGTIPVQ LSGIEKGVKN
RYKDILPFDH SRVKLQGRES GACDYVNASH IKASRSNKRY IAAQGPLPAT YEDFWSVIWD
QDIRVIVMLT AESEGGQLKC HPYWKGNEFG HTKLRLLSEK KVSLDIDKHR SGSNAQMTSQ
PSAEMGRRRA NTTTSTTSLE GATPAPASTS SSDSPYVIVR KFAMSHAAHP FAPIREITHL
HYPSWPDFGA PAQPSHLLGL VELANVMQRA ALPIDTPSVT GPRASSDPPM AWYDEPEADA
QARPMLVHCS AGCGRTGTFC TVDSVIDMLK RQRLARTTLK PVRKRDSDGD IKMSGERQVE
EAVSPKTAQE KAFNFATSPQ RSNRSSPEGK PAWEGPPLNT AWVGDDTVDL ISETVEDFRR
QRLSMVQSLR QFVLCYETIL EYIYRLHEGG SVGAATSGTS RARSGSLQHH RSS
//