ID A0A319DRC5_9EURO Unreviewed; 647 AA.
AC A0A319DRC5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=BO71DRAFT_354535 {ECO:0000313|EMBL:PYH93793.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH93793.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH93793.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH93793.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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};
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DR EMBL; KZ825885; PYH93793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DRC5; -.
DR STRING; 1448320.A0A319DRC5; -.
DR Proteomes; UP000247810; 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; 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:SF82; 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:UP000247810}.
FT DOMAIN 376..489
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71769 MW; 5C924E9D355C8F93 CRC64;
MDKLTTQTSH ITLDSTKSDA PNPEPPFSPA VLSHLDKIYA SLTALSQPNF LKDIQHESDQ
RKDDPLATLA GLYEYMASPE ASAIRPASSS DLSAPLTDYF VSTSHNTYLT GNQLYSDAEA
SSYTNVLLSG CRSVEIDVWD GKGESESAQD DDAGSSSSSS DSDSDEGKTK PLKPRRRSKT
EKLKKATESH PRLHAISEEF EKLEGFLGHH KPSIGSGSSG SSKSVARPEP RVLHGHTLTR
ETSFREVCYA IRDSAFVNND LPVIVSLEVH ACLEQQQIMV DIMEEAWKGM LIQVTPEIEA
RIIPPPVAEL KRKILIKVKH VDSADEDDDR EAKEKAVYSD HMEALKQDRS PTSSVDLANP
SPSPPPRKPS KILQALSKLA IFTKGFHFSN FAQPEAKVPS HVFSLSETAV REAHAKDRDS
LFEHNRHFFM RVYPNGMRVN SSNMDPSFFW RRGAQMVALN WQSFDKGMML NQGMFAGEQG
WVLKPQGYRG SDTQPVTTML RNLDLTIEIL AGQNIPLPPG HTNEHKFHPY VTCLLHVETP
DDDPAAADDD SESEKSGYKH TTQSATGASP DFGAQKVQFP TVSGFVDELT FVRFKIKDNE
FLRDALAAWA CIRLDRLQEG YRLIRLCDPS GSETEGALLV HITRAFV
//
