ID A0A2A2JMJ9_9BILA Unreviewed; 525 AA.
AC A0A2A2JMJ9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=WR25_26746 {ECO:0000313|EMBL:PAV62908.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV62908.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV62908.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV62908.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV62908.1}.
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DR EMBL; LIAE01010339; PAV62908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JMJ9; -.
DR STRING; 2018661.A0A2A2JMJ9; -.
DR Proteomes; UP000218231; 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 Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF193; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00149; PLCYc; 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:UP000218231}.
FT DOMAIN 131..246
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
SQ SEQUENCE 525 AA; 60369 MW; B44FA96AA27961E3 CRC64;
MAQQNKMVEI FKEYFKEMLL CQPLENHPLD GRPLPSPEQL KYKILVKAKR CKVPKISRDH
SYDTFATGSL SFSSDENYST VNSKKTLISL GSTDSGESLP AELPKELISL TEQELRCVFI
PEKEEISYTQ LSSLVNYMEA DRPANFSLAE RRPHILCSVD EDVSWRYFKE KRASHLLKIT
TRRIVRVYPK NFRICSDNYF PMNHWVMGVQ MVALNYQTPG IEMLLNQAMF ERNDSCGYVL
KPECMRNPWE LIDIHSSTPQ VPNRSSVVLK IKILSGHFYS HIVKPSALQR YSCPLLARQQ
SADPITTYVT VQVFDLPEYE KPKCYRTKEA TEEATVTKYN HKSSSKIFLF EKIVLSELAY
VHFCVWQKVG CHSVPVAHKL IPVEKLNNGK SLKGFENVER DTIFCPTESY RNITLRNVNN
QCIGPASLFV LFDVHYFSTQ RAISRALALP FDDEKRERDF VTAVINPFMS EPEERPIMKL
EELDGHMDIE SSNISNLSPT ISNLYQRKLS NTQVTPTKSS GNLLK
//
