ID A0A316V3D1_9BASI Unreviewed; 838 AA.
AC A0A316V3D1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=FA14DRAFT_150181 {ECO:0000313|EMBL:PWN32040.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN32040.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN32040.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN32040.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; KZ819606; PWN32040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316V3D1; -.
DR STRING; 1280837.A0A316V3D1; -.
DR InParanoid; A0A316V3D1; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000245771; 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; cd08558; PI-PLCc_eukaryota; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
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; 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; 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; 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; PS50004; C2; 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 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:UP000245771};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 151..186
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 500..626
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 634..817
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 94610 MW; 221AC12194448948 CRC64;
MLKVTSRKVM QRVVRIDADA GQILWDSKKN NRVNLESIRE VRSGSAARSY RTSLSIAAAH
EQHWISIIYQ ANSIYKALHL IALSDASLDR WYTTLQAVQN ERKLLASCVD MSERRQSIWL
RQQFKGADTS KDARLDFGET VRLCRRLGIM SNREDLRKRF DEADKEGLGY LDFAKFQHFV
AFLKRRVEVE EIFNRLADTM VKVISQTAFF AFLRNEQGHL GINSQAMVDT YRRFRTTVSS
TEEGISYDGF LAFLMSKTAE ALIAISGQVS VTQDMNRPLP EYYISSSHNT YLVKGQLTGE
STAEGYIRAL MQGARSVELD CWDGPGNEPV VTHGHTLTSK VPLRDVIQAI GKYAFVASPY
PLILSLEVHT DLVQQDAIAE ILRTVLGDKL LQYPLEGHSN STLPSPQELI GKILVKAKNI
LLNKKPEEPE KFEMVIKDKN VTSTTDTTTE SESDGLLHNA RDLVRSVTQK GRRLSSKGKM
SDKTTANASG EKKKVMSPAL ASLLIYTVGV KHRGINKKED YAIEHMISLS ERTALKYARS
SSNGVGHNWE DLIKHNRTHL TRIYPSMNTF ARLNYSANFL PNIFWRLGCQ LVALNWQTVD
LGLEMNQAMF MRNGRSGYVL KPEALRKKEK YSLSDPLNQK DQAENTKSVT FVTVTITLIS
AQQLPRYRHK KGNESDGQEK EADMTVLDPF ISLAVIVPDT PSFSVSPNST NKTSSAISST
ESVRSDKEAR TSTVWQNGFN PIWNETLSFR IRLPTNTSSG STDLRNSVRG LLDLCFIRFE
VRNETKRDQI DDVPCLATFM ISLGALEQGY HHVPLYDTSM TQHLFSTLFV HTKLQIDE
//
