ID A0A428RUL2_9HYPO Unreviewed; 1127 AA.
AC A0A428RUL2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN ORFNames=CEP52_017257 {ECO:0000313|EMBL:RSL81169.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL81169.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL81169.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL81169.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
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:RSL81169.1}.
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DR EMBL; NKCK01000483; RSL81169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428RUL2; -.
DR STRING; 1325735.A0A428RUL2; -.
DR Proteomes; UP000287144; 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 CDD; cd16207; EFh_ScPlc1p_like; 1.
DR CDD; cd13360; PH_PLC_fungal; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR037755; Plc1_PH.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 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:UP000287144};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 788..906
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 54..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 126361 MW; 256EA232137156D8 CRC64;
MSLSSDLDSK NTLTITSLHK LSDMSSLTRS HLTQVQTTFP SHTQPVPIPM SAISASSVAS
NSQQGSPIMS PDTAVLTTNS SAQPSPEPMR GREEEVFPSS FQLPESVLFR KMSENSSGQS
LTSNPSAMSE AVGGNRSIMR RLSNRAHRFA TSRRRQSSAA PASRDGSVGP SILRRRSDSN
ATAPPESSVL TDTDEEVEFV PDDSISFVGL DGAVYTSSAN STHGSISGSA GAMAGPVLPA
ELRNGSSVLK VSRKARPRKI NLIYETETNK LSWDPARPHK SLHVDEIREI RTDSDIQQYI
LDFGMAQITE ADKNLSDNWF TIIYTVPESS KTKFLHIVTD NIASRILWTE FLDAMLRYRQ
ELMTSLMAFN DRAIAQYWQS EMAREFGDTP RGTDQEELDI AGVKRVCQSL HICSSQSTLE
VNFHLADSRR RQKLNFTEFK DFVRRMKQRT DVQRIIRSIA ANPELGLTLA EFLDFLRDEQ
GEDIDSNRAS WEKLFSRYSR RYRTDEVDTA ENAQIMSEDA FVGFLTSEDN GPIAPEPQEY
TLDRPMNEYF ISSSHNTYLL GRQVAGQSSV EGYISALVRG CRCVEVDCWD GYNGQPEVNH
GRTMTTSISF KEVMTTINKY AFIKSKFPLW ISLEVHCSPS QQATMVEIIK DCFGSRLVTE
TLDAFPDKLP SPSELMERVL IKVKKPQIKE EVVSAGNDFR GRRRGNSLNS PMIRPTVPDS
AAIMPSQSLP QSPMLTPSHS TRRLVSKTRV NTITEGQVQD MMSSSTSDNE SGAEQAAKKA
PNKTVKVLGD LGVYCAGVKF SGFDTVDAKQ YNHIFSFMEA SFAKHSRTKE QKMALDIHNM
RYMMRVYPDR TRITSNNFDP LIYWRRGVQM AALNWQTFDL GMQLNRAMFD GGKDYSGYVL
KPAELRDIQV LPYNSDIAEG KKERSVVTFS IDVISAQQLM RPANLPANKA INPYVEVEVF
RANDKRDKKE SECILSLEPD SPPKVQTDIK PENGFNPMFD KHFKFRVTTK HPDLVFVRWS
VKLSTDGESF NERPAVATYT AKLTNLKQGY RTLPLLNHAG DQYLFSKLFC KIKVDPVAKK
LIDAPKRTQD GGNKLNRLGG KVFSRINTSP KSTIEKSSSE KTSFDSY
//
