ID A0A1J9RSU2_9PEZI Unreviewed; 694 AA.
AC A0A1J9RSU2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=BKCO1_5400054 {ECO:0000313|EMBL:OJD30932.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD30932.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD30932.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD30932.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-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:OJD30932.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNUE01000054; OJD30932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RSU2; -.
DR STRING; 236234.A0A1J9RSU2; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000183809; 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: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; SM00239; C2; 1.
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:UP000183809};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 394..507
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 77058 MW; 2F448399BDC94AC1 CRC64;
MATDLATTVP QATEGRAGPE SQSVANTPAQ AGGGTASYTI KNAQKVDRLN ATLSGHIDKI
YKKLEKEYEV SNKIGLYNFL VNGQSHSAGA LPIQDEKLTA DSLKSYFRSH HVNALGAAEP
LDLSWPISNY FISSSHNTYL TGHQLYGESS TDAYKNVLLR GCRCVEIDVW DGDAPSDSDD
SSSSSESEAE KDGKPGKTRR LKDRFKAKLG KKDSTKNDPK KKETPPAANT SSARQSQPDR
PKPWRANSNR AEPKVYHGYT ATSDISFRSV CETIRDYAFV TSELPVIISF EVHTSPEQQE
IMVEIMNETW KEFLVDHPPA DQASPASLEL PPLEKLLRKI LIKVKYAPPT KPGETTPPQE
SEPTTPSESE EDATTSAAAT ETPQPAKSKI CQNLSRLGVY AWAIRFQNLK QPEAQYPAHI
FSLSEGRLME VHQHSPAELF EHNKKHMMRA YPKGTRVSSS NLDAPVFWRQ GVQIVALNWQ
RWDEAMMLNE GMFAGTAGWV LKPEGYRSTS QAAKHLHALT YGMLDLTIEL FCGQDVPLPP
DESKAKNFHP YVKCELHVEK PEERLGEPIP GGGKSKEGEY KQHSKTVKTQ DPDFSGEVLR
FEGVPGVTPE LSFVRFKVMD DEFGRDDLAA WACFRLDRLQ TGFRLIHLFD AEGVQSKGVL
LVRVTKNFVA ETPPPSKKGE SVDAVVEEVK KLQT
//
