ID A0A158Q6F5_DRAME Unreviewed; 565 AA.
AC A0A158Q6F5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=DME_LOCUS3508 {ECO:0000313|EMBL:VDN53535.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000995701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000995701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN53535.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYYG01000142; VDN53535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158Q6F5; -.
DR STRING; 318479.A0A158Q6F5; -.
DR WBParaSite; DME_0000995701-mRNA-1; DME_0000995701-mRNA-1; DME_0000995701.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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; cd16200; EFh_PI-PLCbeta; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.30.29.240; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR037862; PLC-beta_PH.
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 PANTHER; PTHR10336:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00148; PLCXc; 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.
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:UP000274756}.
FT DOMAIN 328..479
FT /note="Phosphatidylinositol-specific phospholipase C X"
FT /evidence="ECO:0000259|SMART:SM00148"
SQ SEQUENCE 565 AA; 66285 MW; 778BE1A1C54CC1F1 CRC64;
MAKEYQFNWK PNIPPALIDG TFFDRYDDES TCLDLNAHVC IDDYGFFLYW SCEGKDAVVI
DLVQLWEARV AGLPKDGRIL FELEQRGPRE TLEERTVWIT YGLDLVAVNS FYIVAQDIEI
AKLWRNGINE ILKNCKMKHI SYMTSLMKNW RYLCLSLNDR RKIAIKNIVK MFISGKTEKM
VQKCLSDLGL SGDKVGEIHI QFKNSTKCFQ EREELDVELF TFEKYLRLYY KICPRTDVQE
LFVRLSGQKE YLTMERLINF LNEEQRDPRL NEILFPFFDQ KRTQQLINKY ETDENYVNNG
KMSGDAFLRF LMSNENAPVF LDRIELYQDM DQPLCHYYIN SSHNTYLTGR QYGGKSSTEI
YRQVLLSGCR CIELDCWDGT GDNKGEPIIT HGKAMCTDVF FKDVLYQIKD TAFARSEFPV
ILSFENHCSR PNQHKMAKYC MEIFGDMLLS KPFDDYPLEP NIPLPSPNRL RKKILIKNKR
LKSDIEKLQM DQFLREGKLD EEDEAIESPE AVVGEDIDAP REDIQIKEID EAHPEFKSNF
ISKLKPLSFT KKPQVFLNIF QILIF
//
