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Database: UniProt
Entry: A0A1I8CG98_9BILA
LinkDB: A0A1I8CG98_9BILA
Original site: A0A1I8CG98_9BILA 
ID   A0A1I8CG98_9BILA        Unreviewed;       883 AA.
AC   A0A1I8CG98;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000418600.1};
RN   [1] {ECO:0000313|WBParaSite:RSKR_0000418600.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000418600.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I8CG98; -.
DR   WBParaSite; RSKR_0000418600.1; RSKR_0000418600.1; RSKR_0000418600.
DR   Proteomes; UP000095286; Unplaced.
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; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
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:SF196; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 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; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 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   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          378..469
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          467..593
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   883 AA;  100331 MW;  F399017A0B43A2CA CRC64;
     MSQSARAVFY NQPSVTSVSG AEILRAINDK IVVPRIKQKL KEVIASQDDE FRGRISMAEF
     VDMYKDLATR PELYFLMVRY ANKDYLTTED LQLFLETEQG VSDVTKEMCE EIILKCEPSD
     EGKNNSLMTV DGFTNFLLTK DSSVFDPAHL NITEDMDHPF KNYFIASSFN TYMVEDQVKG
     PSSVDGYISA LKRSCRVIDL DLWDSIDIED KNEPMIHNSQ ISSCRLPLSA ALQVIRDLAF
     ETTSYPLFIR LEIHMSLHYQ RLAYEMIEDI LKELIYHPIE DVRDWTDDKN VPSPKRFQNK
     ILFIGKKYSS ESDVGEVIED DKSTSIMGGK KVHSPKIYIL KEFSDLIPNF LEAINVKKEG
     INATDVNSLS NYDLIPKHHL VTINEGDCLR IMQNYPADLT QVIKEFITRA APDTLRVDSS
     NLNPQEFWNF GIQMVALNYQ TPGLMMDLQE GKFSANGRCG YVLKPAIMRE DLFAPCDRLP
     YSTQILHLRI LSGQTLPRPR GSTVKSDSAD PFVVVEIFGI PSDCAEERTK TVRNESVNPN
     FDESLQFQIS VPELALVRFL VLDDDFVGDD FIGQYTIPFE CLQSGYRHIP LLNSEGDLIE
     NSTLFIHIAI TNRRGGGKKQ KRGMSVKLKT NRIQTGMKQI GIKSVDELFK AAVLPLVESI
     EMRNKMDYAL SNWQEQTGLN SMGTIRQGLR LMYSRINSIN TNGTPPVSTK LFHRDNTQNK
     FEEHIPPSFY FEPNEVGHPV MKRRGVFPET LLKTFSSMEA LFEKCSIILS KTDSLLTKLE
     EATKKIGECY EDLPDICITA GLRSQKATRA TENFAWNVRL LKSQLALMHK SQLEASDIFT
     QVFDTAKLLG ILKNNNVNNI NNSNGDKLHS KAESYEDVND VQL
//
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