ID A0A427XE16_9TREE Unreviewed; 580 AA.
AC A0A427XE16;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=EHS24_003916 {ECO:0000313|EMBL:RSH76977.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH76977.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH76977.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH76977.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
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};
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:RSH76977.1}.
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DR EMBL; RSCE01000019; RSH76977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427XE16; -.
DR STRING; 105984.A0A427XE16; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000279236; 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:SF169; 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; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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:UP000279236}.
FT DOMAIN 340..428
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 16..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 63913 MW; 2F439581A0BA372D CRC64;
MVDLASRLAS LSPFGRKQQL DTDDSGELVD SGSIAGGGHA GRHTELQDSL RVSEALRRFL
AHEKVIRDDK PDSPTLSPTL HALLQRPHIQ VPPELTDRSH PLSAYFFSSS HNTYLKAHQL
FGASEVSAYG STLAAGARCV EIDAWDDEAN ADEPKVTHGY TLVSHISFRA VCEAIRDVVD
KEAQSAASTQ SGAAAPIFIS LENHCNPHGQ KRLVNIMQEV WGDRLLSSDV RRKGHEEQEG
GAKVRLDELG SKIVVIAEYY FPGETVPDDD DDDDDEGSDG DSGEQEDTKK ARAEYAKKKK
ATTTTVIIPE LADIGVCAQS CKPPNNSWFE SELVDGPHDH LINVSESALS TLLSPHKDMI
AAHNANWLMR VYPKGTRISS KNLDPVPFWG IGAQICALNW QSFGPSMQLN EALFSGTDGF
VLKPSYLRGG EKLPSKRKRL RLRIAGATDV PVPKGRESDD IKPYVSCVLI HPDDLSGKPP
KCKTDHYKQA HIPFLRPGHK SPVTDPLWDE TLEWVYADDE LVFLRMLLKS DDKFAANPTL
ATAAVRLHYA VKGWNFIRLI DPRGHETTCT LLVKVDIDDA
//
