ID A0A2C5YV58_9HYPO Unreviewed; 567 AA.
AC A0A2C5YV58;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=CDD80_3827 {ECO:0000313|EMBL:PHH73425.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH73425.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH73425.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH73425.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH73425.1}.
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DR EMBL; NJES01000344; PHH73425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YV58; -.
DR STRING; 2004952.A0A2C5YV58; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000226431; 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:SF169; 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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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:UP000226431}.
FT DOMAIN 294..412
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 62722 MW; AF3AB0CD93EDB3EB CRC64;
MADLSSRLGR LKPFSRGPDD EDDYDDIDDG GEVTGQDAIG GGGRYRRNAD HEVESLKVSD
ALQSLLVDRG VLPEAQGDDR SEVLAKLLDQ NDCCVPDRLM DGSRPLPEYF VSSSHNTYLL
AHQLYGTSSA EAYKTTLRMG ARCVEIDAWD NAADPDEPKV THGYTFVSHV PFRAVCEAIR
DIHDEEKEEI ESDPTFPVAP ILLSLENHCK EHGQRRLVAI MKEVFGSRLL CEAIVKDAPP
DEYASPADVG LLIAVMVEFH FDDAPVDDCS TCSEDDSTTE ATPAEAQVMI VPELAELGVY
AQSVKPLDNS WYDPGELVNG PHHHLINISE TGLSKHLPAN GAAIAAHNAR YLMRVFPKGT
RISSSNLKPV AYWGIGAQVC ALNWQTFGTG NLLNDALFNG SNGYVLKPTA LRPGGSGILG
SGRRRKLRLY VAGATDVPLP EGREADSIKP YLTCVLYSPC DIEGATHKRK TSAYRQHRLG
FLHRGENPRP TDPIWDETLQ WKYEDNELVF LRLLVKSDDP WARNPAFAAA AIRLDYAEAD
WCFVRMMDMK GRETDCTVLV RFGFEDL
//
