ID A0A2J6TFZ4_9HELO Unreviewed; 1057 AA.
AC A0A2J6TFZ4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=K444DRAFT_525660 {ECO:0000313|EMBL:PMD61930.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD61930.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD61930.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD61930.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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};
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DR EMBL; KZ613785; PMD61930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TFZ4; -.
DR STRING; 1095630.A0A2J6TFZ4; -.
DR InParanoid; A0A2J6TFZ4; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; 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; 2.
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; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 338..373
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 711..829
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 835..994
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 118308 MW; 99DB6394F496703A CRC64;
MSPETTQLTT NNSSIQGSPD SVRGRDSEYP PPPFELPEST VSRKSSQSAM SEALVMNKSP
GLIRRLSNRA TKFAGRRRQS STTAMSRDHS TGPVTMRRRS DSTNTAPEGG KGALFSDSDD
EFVVDMREEY YYPLALDGKG DYPSTTASIG SSTVPSATPP PGPVIPKVLL QGTTMMKVTK
KKKKLLTFVL ESEAAKVCWD KNRPSKSFYI DDIKDIRAGA DARNYRQEFG VAAADEPRFF
SILYAVPDRS KGKSQQKIMH LIANDDQTFD LWTTTLDAIS KHRQDLMASL SSFNDKAVRA
YWRTEMNKQF QDKPHLEDEE EIDIVGVERL CRSLHIHGSS SYLRTRFDQA DVSRSGRLNF
VEFQTFVKLM KRREDVRAIY RELASDSEKG ITSEEFFRFL TDIQFENVEA DVAHWEDVFA
KFARRSKPKD AVEGEASRMN EAALSSYLIS TFNLPLENIA ATHTLNRPMN EYFISSSHNT
YLLGRQVVGQ SSVEAYISAL NRGCRCVEVD CWNGSDGQPT VMHGHSLTTA VSFADVMSTI
SKYAFVKSPY PLWISLEVHC NSQQQAIMAE IIKETCGSKL VTQPIDPSVE QLPTPSELMH
RILIKVKKPR SFEDSAVMEQ TNGRTRGSSL SSPYVRPTQL DNSTISAGLL PPTPYSRTYR
TISRGQPKYS GSEGQDSLSS STSDSESLTE DVVRAKENKA KNKTSNIIKV LGELGVYCAG
IKFQGFDAPE AKSYNHILSF AENTFDRNTK DPEDKRAVAR HNMRYMMRVY PSYKRIYSNN
FDPLKYWRRG VQMVALNWQT YDLGMQMNDA MFAAGKDQSG YVLKPIELRE IKMIPTVPEE
AGVGYVRRER KNVTFSIDLI SAQQLMRPKG LAPNQSVNPY VEVEVYHADD KSKDSKGVVG
EGGLDASAKD GFSGLGTPHR RRTQIIQDNG FNPIFDKKFN FALTTKYPEL VFVRWTVRCS
NDGSGYSEKG SPLATYTAKL SSLKQGYRTL PLHDNSGDQF LFSTLFCRIK IDPATSIYVN
GPESAANDSV GVLKNISRTV WNRTPMSPKT SVDSGNS
//
