ID S0ELB2_GIBF5 Unreviewed; 1088 AA.
AC S0ELB2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FFUJ_11870 {ECO:0000313|EMBL:CCT75828.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT75828.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(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; HF679033; CCT75828.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ELB2; -.
DR STRING; 1279085.S0ELB2; -.
DR EnsemblFungi; CCT75828; CCT75828; FFUJ_11870.
DR VEuPathDB; FungiDB:FFUJ_11870; -.
DR HOGENOM; CLU_003457_0_0_1; -.
DR OrthoDB; 1430740at2759; -.
DR Proteomes; UP000016800; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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: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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 901..958
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 614..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 121180 MW; 1D5D4D1FFCB29DF8 CRC64;
MKLSRVTPFT LLAASYQAAY VQFQDCADTL TNKSLIPESF RAAVEQGRDG FEWRFDVIAG
QADRNACEID VGDVVPRFTV IDYGRDSKEV SGEIVNMSCY TSEWLGPRAH FTIASSFKRS
AFLDTFRTTL EITSKDNESL SCVRATLTPA APESIRLLSL WLPIATFALT CIVACWPAQQ
TTSSLTSKNG RITRAINLLA YIQFVFFSGA HSLRYPGFFQ PLVGLCSWST LMLPAGPVEA
SSPYARAGVN DGIYEHNGTI TGAPGLELLT QMTGSPVKPQ SWMNTFVLSL IIFFFLYLSS
YISFRLNSRD SPSNLTLATI GSQLRDRYWA VVRLFLSCFM LPISAWATYQ FLDDQIFGYR
NSAMAILILI VLLAGFWWSW TRDSEMGSLV IQSPGRLNKD PESGRQYYAL VLFSLMFLRG
SVIGGLQTYT SVQLGVLLGC ELLQLLAMTF WTRFACFISL AGILSVSRLA LFALHIGFVP
GLASHSGRML VAYIILCGHV VVLTCIFLLP TVLDMAHLIM YGRAVTMSDA DRGTPVREVS
RPIQRAQTDI EGLQKSKSAK TRDLNSHTRA SPDFNQLLLE MILKRETNNL LIVLTSQKAL
TEFLEDLKGR DNRAESEKNS NVFSDSSSTL INPSSSKEEI APVSDISGDL VSHLFSKENL
AIRSAPRHHN LDYPINQYFI SSSHNTYLRG RQVAAPSKLK GYISTLSQGC RSVEVDCWDG
RDGQPIVKHG YSLTTSISFR SVIETINNYA FFASDLPLWL SLEVHCNPAQ RDIMARTMLE
IFRSSLVVEP LDASSQELPS PNQLRGKILL KVKVAQDPEP LQEPLAPEYL NLDEPGEYIE
NQDHQDLPGD LLQSLAVYGA SRRLPKNAEF DTHRNFIYSV SERNFKKHTK DNCSLDLAGT
QHLVRVYPDP NRVDSSNFDP LQCWRHGVQM AALNCQTDDF YMSLNQAMFH GSSGYVLKAS
PQTTQIQLQV DVLMARGLKV STGNGPVHVK MKLLTPDTMS QKARTAPVLL QDSDVAFDEN
LEMSVETNYP HLTFLHWSVK TMSNGRSMSI TSGTAKVENL REGYRVLPIG EASNNKGRLL
CKISVKST
//
