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Database: UniProt
Entry: A0A094GIU9_9PEZI
LinkDB: A0A094GIU9_9PEZI
Original site: A0A094GIU9_9PEZI 
ID   A0A094GIU9_9PEZI        Unreviewed;       809 AA.
AC   A0A094GIU9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=V498_02974 {ECO:0000313|EMBL:KFY96015.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY96015.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY96015.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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};
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:KFY96015.1}.
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DR   EMBL; JPKA01000488; KFY96015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094GIU9; -.
DR   HOGENOM; CLU_002738_3_0_1; -.
DR   Proteomes; UP000029270; 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; cd00275; C2_PLC_like; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
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}.
FT   DOMAIN          550..663
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          86..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  88649 MW;  D240D19B08EC0AC8 CRC64;
     MVLVSTLLCA GRQTQGWASS YSQTGAPIND VGRVQAVPAI HSARGWGTEA EFSSRDLYLR
     GDGRQHWQRH QPRPPLPIAA TISPTFAQQT HGTPQSQRRA QAPPLLPLPR LNDYPHGTNA
     PPHGALAAYA ALPLARRASA PAENLHHPVR GLAGHDIPLS EDVEEYSYED WLALLWMKGG
     LEAVGALTGS KDLGKPISSY YISSSHNTYL SGNQLMSKST TDAYKNVLIR GCRCIEIDVH
     NGEPVSTSSR RPHITGTTPS DLAVSAIQAK KKYKRKYKTE YKAKLGALKG KIPWSRSDDK
     KEKAATAVTD NVEPIHLLGH KKTVSNVPSI NREKTSDSDS SSSSSDDDYD LADGSRSRSS
     SVLKGEPVVL HAWTLTRAVG FREVCRAVRE SAFQTTNLPL IVSLQVGCDL DQQEVMVQIM
     KEEWEGVLVD TAHPTCHPEE RLPRLDELLN KILIKVKRSS EVPPSEPPSP NVSMATSSNP
     ITPLSASTTI SSRPSTLTPT ATISTPLSPT TSNDNLDALS ESSRSRSPSL SRSRSRSPAP
     KTKARMHPSL SALGIYTHSS HFSSLTASSA STPSHIYSLS EGDILELFAA SPNALLAHNR
     SYMMRAYPAG HRIDSSNPDP SVFWRKGIQM AALNWQVWDE GTMLNEAMFA DSDGWVLKPP
     GMREGGELVE LDAQKVDGKL LDLRIRVFAA QRILGEKELR ARVKVEVHAE RAGEKAGEEW
     KRHTETKRGA SVDWEGERLD FLGAGPGVVE ELSFVRFRIE DDGFTDTLAA WACVRLDRLQ
     NGYRFLKLRD AKGAATDGLL FIGVEKIER
//
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