ID A0A2T9YM39_9FUNG Unreviewed; 1007 AA.
AC A0A2T9YM39;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=BB559_003288 {ECO:0000313|EMBL:PVU93413.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU93413.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU93413.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU93413.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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 -!- 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:PVU93413.1}.
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DR EMBL; MBFT01000323; PVU93413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YM39; -.
DR STRING; 61424.A0A2T9YM39; -.
DR Proteomes; UP000245699; 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; cd08558; PI-PLCc_eukaryota; 1.
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; IPR011993; PH-like_dom_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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 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; SM00148; PLCXc; 1.
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:UP000245699}.
FT DOMAIN 539..653
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
SQ SEQUENCE 1007 AA; 115580 MW; 0691F5457B04D402 CRC64;
MTSTNSQETI HFYPLYNTSK VISNIGICTL PKDQVISDHK QKIRKIAEIS SKKYLILKAT
SRKLHYKPFR LDFQQQRIVW ESKKNRFNNK VDLERIYEIR FGQSAEETIK IPSNISEKLK
ENIIVISYIR KSEHKTLEIF TQDKQDFTEW IFFLQVVLNS LTQIQSTEDQ KIWDSVIAAR
QNWEYDITRK DNYFYTESQK DIPNVLDQNS RPTIPLALPN KSKRIIGNFP RWGIFESGRQ
QSVSFYEKIS GLNREINEHS LYKKNNFTYI LNECYKENLV TFGKKHEFQY KDFKNFVLNI
QKDKISDAQI KKIFYSYSNS SGIITKKCLL NYLKSSHNSI TFEPPPKTAL IDLNEHNTHY
QQINMDKPMN EYFISSSHNT YLLGGQIIGT SSIEGYIRAL HKGCRCLEID CWDGPLGEPV
VCHGRTFTTR IPFKDVIEII KSYAFIRTPY PVILSLEMRC SMPQQVKVAN ILKEVLGSAL
VTTRIKSKTA IPSPNDLMFR FLVKNKIILG NSRNSSSNNV FKQQQTHKCY NSSKVAKELS
DLAIYFQAMH FEDITDNYTK NGAIVSVSES TAVQIKNSNP NFLYEKSCLN FIRIYPSFSR
INSTNFNPVP FWDSGVQMVA LNYQTFDKNM QIHDAFFGMS YGTGYVLKPP HLRNLESENN
IDIDREHSLR SVNESTCNLE SDGVFASVDT KTNNDGNFLK HQEIIPKTEC KNQFAEPRKL
IVKFLNASVG KEVKSTEMKS GISCQIELIY DMQKGPFAMI GTYDFGNDMK KTNTFLTSNG
NSDRYDSFSS GGKASEKEYP DTDFKNHKNY FIGNFDFEES KSLSKKSSKN WEVQTNKEEI
KENLEYLQQK KVQNPRKIGF SVPFAKSCKG FFGSEIFSSP KKKSVSVKSL KTNLSNASTS
ISTTTTIIGQ ANNTTYQTEY TQLASMSEGF WKDTGCIALI PRTKIIICRF SIRALGKGGV
GETEIASACI PIEMLKVGYR QIELQPNWSS GAFIGESLYP FMFVRIE
//
