ID A0A1Y1W259_9FUNG Unreviewed; 1125 AA.
AC A0A1Y1W259;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DL89DRAFT_294760 {ECO:0000313|EMBL:ORX67620.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX67620.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX67620.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX67620.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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};
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:ORX67620.1}.
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DR EMBL; MCFD01000012; ORX67620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1W259; -.
DR STRING; 61395.A0A1Y1W259; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000193922; 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; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR035892; C2_domain_sf.
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; SSF50729; PH domain-like; 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:UP000193922}.
FT DOMAIN 703..805
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 432..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 123151 MW; BCB1622A1989D9DC CRC64;
MVSKAQTRSE EAPHRLHHYC SHSHMRDRLK SSGSRSTDMC LPCKRQHVIG AFSRVRRVPT
RLLSTLSLSS HHHGPSGCTA GANAGVASDG DLHTDSLESK VYPVYSARPA VCLSSHADAL
ADPGYVPLPH VPPALAAGCS LMKTTSRGIH ARNFRLDIAQ QRLTWDSRKK KKLAHVDLER
IIEVRVGEEA LWSVGDPACL PNRTKNLFTI VYYQQMAIRS LCLCASTESL FRDWVVTLNA
LVANRQPVST LPLFERWRMI TINRQWWESD TSGDAATDAL TFVENAFIAS RTSPLTTAPS
SNASSMLALS AVSHDVPPPI ARAMSRPASP VKQLPHRLGS MVGLRALQLH PSLPPPPPPL
LTRALEMVPQ RVGCCDEVVN DLVEAAIMCQ ARPDVAAIYS NLVTSALMQE AAKNSLKQRQ
RRVAVVPSTG FGDKQFRIGD DDDDDNDEDD GEDEFGDFEP SIYTDSAESS VHRPSELTLP
MFAHFVREEQ DEQVSDAEVE RRFDAFTRTE GQETMTPFEF EAYLLSLYNS MDYVEGDYAN
SSDSSDGRST LSEHAELANM DEPLNHYYIA SSHNTYLLGI SCTTRILFED AIIAIAKYAF
AVSPYPVILS LETHCTVELQ VKMAELMVEH LGDYLLTEPL NEDETELPTL EQLKYRIIIK
NKVLEEHASR SNSRRSSIIG IQPSTLLAEG PVKAKGGKIA PELSQLITYC KAQHFESLEE
NLAAYDQVSS IDEKTSGSLI RNQRAKFVEF NSVQMTRVYP HYRRIGSSNF NPISHWNTHD
RAMEIYEAMF RRTHNAGYVL KPQHLVAPSP AVSSSSSTYS RSSSDSSSDM SHPRPLASNP
AAHPRRATVH LTLFAAYNAA RSTGHVGNAG AATDSGFRHS GGTYFDMPST PRALSRPPST
IAMFRAEPNQ LALDSFAFGS PSLAAAQAPG GSGFLTSSTM TPSRPGHHMP RFRVEIELIT
DGGVGKGGGL TATHSSVEDL TALASALNSA PGSPTLNAQH LTSFPFGSAA GTGGASAVVP
QPALHSLVLG RSRYCTRNGT VSCGVVRWRD EHVMHMVRDP DMAFVRFAAF EDDQEVASAC
ILVAALKNGH RFIELGESDK HRLSRPICLL VHVQGPAHSR GARTP
//
