ID W6ZM80_COCMI Unreviewed; 1113 AA.
AC W6ZM80;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=COCMIDRAFT_21499 {ECO:0000313|EMBL:EUC51113.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC51113.1};
RN [1] {ECO:0000313|EMBL:EUC51113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC51113.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KI963919; EUC51113.1; -; Genomic_DNA.
DR RefSeq; XP_007682329.1; XM_007684139.1.
DR AlphaFoldDB; W6ZM80; -.
DR STRING; 930090.W6ZM80; -.
DR GeneID; 19120072; -.
DR KEGG; bor:COCMIDRAFT_21499; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_1_0_1; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000054032; 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; cd16207; EFh_ScPlc1p_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; 2.
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; 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; 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; 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 744..863
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 863..1017
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123913 MW; FF333F71AA86F1CC CRC64;
MSLLHDSYAR PRMPSPSPSY ARAISISARG SPALTASCLN GSLQSTPEGM VPISSSLPAI
PSYTLPESLL PPPVQSQPTS SPSAMAEALG KGPGLIRRVS RGAQGIPHRF RRGNSTAQRD
KSSGPVIMRR RSDSRTAADG DTGISDFDAF EEEEAIEDPY EPIHGLGITG PSPSFSSIPD
TAVVAPVRNS RLEQGTVLRK ITKKEKKEIN LRLDLESAKV FWDPSRPSKA FYIDDVKEIR
SGPEAKHYRE ECGLSENWAP YWFTIVYTDT TRSKGRIRTM HLIAPDVGVF NMWTQTLESV
SRNRIDLMAG LMGFADKSAK LVWQRAMKKR GEGEESLDFP SIVELCRSLH INCSEATLRI
YFQKADNQST GKLNQQQFLS FVRRLKERKD IKTIYKSLTS GSKIEMDKVT FFSFLQQEQG
VDVNADLEYW TNTFERFARA TKPRAPATPV EGGDIPLPLA MNFSGFQTFL TSAANSILRP
VGRQQKLDRP LNEYYISSSH NTYLLGRQVA GESSTEAYIT ALQKGCRCLE IDCWDGADNI
PVVMHGRTLT KSILFQDTIK VINKYAFTES PYPVILSLEV HCSPVQQSAM VKIMMQEFGD
KLVLQPLDFE SQSLPSPEEL KYRILIKVKG AAGDEFDTRA LIGEITSRRQ RSFSSPWSRP
VIMNDNAIPN SPLLSSPPSM SPPERSATFW ATPRTSNNTL PTSTAVSSAE DSDSPNATAA
EAAEVVDDRT KSKKAKTSNI TKELGSLGVY TRGVKFTDFG SMEANTFNHV FSINERAFDK
LTKPGAREKH LLEEHNMRCL MRVYPHAFRI NSSNFDPLKF WRRGVQMAAL NWQTYDLGQQ
LNEAMFAGGD DRTGYVLKPA ALRLESQTPV VGHRKAPKKQ VKFTVQIISA QQLPRPRGLG
QEANINPYVE FEMYCAEDMG ANATGIGGQD ASARNGHSGI GNPLRKRTRI VEGNGYNPEF
GNEIDMTVTT RYPSLVFVRW TVWNSLDART TNHAPLATFT AKLSSIQQGY RHLPLYDSNG
EQYLFSTLFC KIKKQDIVDA PEVSSGTSCG SSIDPGSPLQ EPTNTKASRS FVRRLISRAP
SERRRRKEEL HRTGSESRES DLDPISRSST MER
//
