ID A0A0F7S0Z6_9BASI Unreviewed; 588 AA.
AC A0A0F7S0Z6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=SSCI48030.1 {ECO:0000313|EMBL:CDS00652.1};
GN ORFNames=SPSC_03126 {ECO:0000313|EMBL:CDS82307.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDS00652.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDS82307.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDS82307.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CDS00652.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) 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; CCFA01002859; CDS00652.1; -; Genomic_DNA.
DR EMBL; LK056665; CDS82307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7S0Z6; -.
DR STRING; 49012.A0A0F7S0Z6; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000242770; 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; cd00275; C2_PLC_like; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
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; PF00168; C2; 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; PS50004; C2; 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 Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 317..434
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 429..569
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 64573 MW; 7D5A8B75876F595A CRC64;
MSDNQDPNTK DGKAAPSIIT SNFAKLNPFS KTGAADPEGG GDNLGEEVEL DSIAGGGHAA
RRTKITKSEL RVSHALRKFL IDEKIISAAD ALLDDQNAAS SDALKAIVDK SHIDVPEYVR
DRSRPLSEYF VSSSHNTYLL AHQLYGSSSA VAYEHVLVTG ARCVEIDAWD NEDDPLEPKV
THGYTLASHI PFRSVCETMK QAIQKEEAEA QRDQSFKVAP VLLSLENHCG HAGQKRLVEI
MHEVWGDLLI SGPVEKGEPA SEHTALDHLG AKIAVMVEFH PSDQPPVEEA HDDDDAEETA
NKAKRNEAKK AGIIPELCAL GVYAQSVKPT NDSWYTSTLT NGPHDHLINI SETGLLDLLP
QHGTAIKKHN ASHLMRVYPK GSRISSKNLN PVPFWGVGAQ VCALNWQTFD HSVQLNEALF
SGSDGYVLKP PGLRIGGDGN TSLGKHRLTL HIAGATDLPL PKGREADDIR PYVTCTLILP
NDLESQPPKQ KTGTYKQHKL ALVHKGPQPT PTDPLWNESL QWSFDHDELA FVRILVKSDD
KFARNPLFAV AAVRLVYAAK GWRFIRLLDL KGRETHSTLL VKFDLEKI
//
