ID A0A0K6G343_9AGAM Unreviewed; 1028 AA.
AC A0A0K6G343;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=plc1 {ECO:0000313|EMBL:CUA72788.1};
GN ORFNames=RSOLAG22IIIB_05048 {ECO:0000313|EMBL:CUA72788.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA72788.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA72788.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA72788.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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; CYGV01001312; CUA72788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6G343; -.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd13360; PH_PLC_fungal; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR037755; Plc1_PH.
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; PF00168; C2; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 367..402
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 760..875
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 870..1006
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 115740 MW; 028A396363333A0B CRC64;
MAPSTTPQLT LRRAEPLVSA SGELSPALQS PPDTRYTFLR TLPRRRSLKD KVGSGLRKLV
ARAKSFTVPS PTHEDDKPRE YEDAHETGVK ARDFAHRRAA SDSMSSFPRL AHDSQDEDSS
PPKRRPALIL TRSHGSSSTP RVEEEEEEEE EDGSPKAYIA DPDPTPTSTS LFALDEGASS
SCDSEAMVDN PTYIDTGAQA RAQSPVEPIV PSVLVQGTPL LKVTPKKTKQ KFFRLDADQG
IVTWESNKGG IIQIENIKEI RTGKSARYYR EQFKISAERE NRWMTIVYTS DNKYKILHTI
AFSQETMRLW SKTLESIRAL RLNIMSGVVS PARIWERHYW RGADMSDDGK LEIEEAQRLC
RRLGVDPVQA NLIERFKSAD KGGKGYLDFT DFQTFVKKLH SRPDIKRLWN RMRGEGLFDL
AVFGRFMREE QMMTEMTDSE VARIFKKYAT GGTELPTPPP ETDSPTAVSS PYKSKVRSRS
RSRSRSGSFS FSSVPKFKNA QPASPVVCSY PDKESNIPAP HSLTTLHFTL DDFSAFLLGA
DNSAFEDQEH DMTRPLSEYY ISSSHNTYLV GHQLVGESTI EGYIRSLGSG CRSVEVDIWD
GDHEPVITHG RTLTGSVSLR HVAQAIAKYA FVASPYPVII SAEMHAGIEQ QSMVSQICRE
EFGNALITCR LDGTNDLEEL ECLPSPEELK GRVLLKFKNA LLSEVEVEGE IEELDDPTSD
SESIGKAAAT IPTSPPRKKQ RAYSNRSELE RPKLKMSRSL ADLLVYTVGV KFRGLNKKEH
YTVEQMFSLS EKTANKVLKE NWMGLVKHCR TNLVRVYPNG TRVTSTNYEP ARYWAAGVQL
VAMNWQTIDL GNMMNQSMFL RNRRAGYLLK PEALRIKDKD LLAKREDYVL EITIISAQQI
PRKRDENGRE IIKDGLADPL VEVSLHTPVP GATPQTYRTT AIPGNGFNPI WEETVSIPFT
CIADMWDLVF LRLAVMNDDD DDEPLAVYCS PLGSLRKGYR HLPLHDLQFS QYLFSTLFVH
VSLRRAQV
//
