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Database: UniProt
Entry: B2WD36_PYRTR
LinkDB: B2WD36_PYRTR
Original site: B2WD36_PYRTR 
ID   B2WD36_PYRTR            Unreviewed;       614 AA.
AC   B2WD36;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=PTRG_07895 {ECO:0000313|EMBL:EDU50814.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50814.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000256|RuleBase:RU361133};
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DR   EMBL; DS231622; EDU50814.1; -; Genomic_DNA.
DR   RefSeq; XP_001938227.1; XM_001938192.1.
DR   AlphaFoldDB; B2WD36; -.
DR   STRING; 426418.B2WD36; -.
DR   EnsemblFungi; EDU50814; EDU50814; PTRG_07895.
DR   GeneID; 6346170; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   eggNOG; KOG1265; Eukaryota.
DR   HOGENOM; CLU_002738_3_0_1; -.
DR   InParanoid; B2WD36; -.
DR   OMA; SSYRRCT; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08598; PI-PLC1c_yeast; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF82; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT   DOMAIN          393..506
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  68114 MW;  B40F48D91C2EFD20 CRC64;
     MPDLTQDKKL GAPEVENPYL QAGGGTASAT STARHVDNLS PLLTQYLRTV YTDISKHYDL
     TTKEGQLRWL TEEQQCSGKD AELLADGSFS HFANYFMSDS ASVMKPPLPL DESYPISNYF
     ISSSHNTYLT GNQLSSDASV DAYKNVLMRG CRCVEIDVWD GEVLSDSSSD EEAAMGNPGA
     DSLRKEKKKS KSGLSIRKRL AAKFSKKEEP EEKSHEASPP PQDGMQKIEP WHSASFTQRA
     EPRVFHGYTL TKDMTFRAVC ATIRDYAFTV SNLPLIVSLE VHTCPEQQEI MVEIMNEYWK
     GMMLEEPLEP AQDLDSVHLP TLKDLEKKIL VKVKRGHTTP VAPTSQPATT DASRPPLKHT
     ESAASVNSGT SSEVGPDGEK KPPAPKPKII KSLSKLGVYL AGYSYKTLDA PEAKIPTHIF
     SLSEGTLMEV HETDPEGLFG HNKHFFMRAY PKGLRLTSSN LNPSVFWRAG VQIVALNWQR
     WDVGMMQNEA MFAGTAGWVL KPEGYRSTSN AATQKTAIPH HDLDLSIEFL GGQDIPLPPE
     EDDPKDFKPY VKVELHVESH EERNAEPVPG NGRSQKGDYK QKTKTSRSPN PDFGREVIKF
     AGVPGVTEEL TFVR
//
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