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Database: UniProt
Entry: A0A2N6NPB3_BEABA
LinkDB: A0A2N6NPB3_BEABA
Original site: A0A2N6NPB3_BEABA 
ID   A0A2N6NPB3_BEABA        Unreviewed;      1145 AA.
AC   A0A2N6NPB3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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_0 {ECO:0000313|EMBL:PMB69115.1};
GN   ORFNames=BM221_005701 {ECO:0000313|EMBL:PMB69115.1};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB69115.1, ECO:0000313|Proteomes:UP000235728};
RN   [1] {ECO:0000313|EMBL:PMB69115.1, ECO:0000313|Proteomes:UP000235728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEF-007 {ECO:0000313|EMBL:PMB69115.1,
RC   ECO:0000313|Proteomes:UP000235728};
RX   PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA   Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT   "Characterization of T-DNA insertion mutants with decreased virulence in
RT   the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL   Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB69115.1}.
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DR   EMBL; MRVG01000005; PMB69115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N6NPB3; -.
DR   OMA; HWQREMS; -.
DR   Proteomes; UP000235728; 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; 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:UP000235728};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          803..921
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          62..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1119..1145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  127836 MW;  23555FC9CCD690F7 CRC64;
     MVMLYKTARP TPTTLPAKDM SNMSSLTAQL RRRPSPAMVQ TNVQPQHSNS LPISAISASS
     IASSSRQASP TMSPDTAVLT TNSSLQPSPD AFHTRLDDDV CPPNFQLPDA IVSRKTSVNS
     LAQSWTGNGS PLTEMPSNGP ASPTPAPTKT NLIRRLSSRA SRSITGRRRQ SSAAPPARDS
     SVGPCFLRRR SDSNNGAPPD FAPANTDSES DFDDRDEYGS LRTNNFMLDG LVRDAPKPPA
     RNATSPVGGS STTMAGPVIP LQLQQGVWLR KISKKSRSKR IRLQYDPDSN KLVWDKARPQ
     KSLHVDEIRE IRTGSDIQQY GRDFKIPESE RSTWFSILYS VPERSKSKFM HLIADDTEAC
     DVWTTFLHAM LRHRQEVMTS LMSFNDKAIA QYWQTEMAKQ PDFGGATQEL DLAGVKRVCQ
     NLHIYSSPVI VHANFRIADA RARERLNFEE FLEFVRLMKQ RKDIRYIMHC NSANPEMGMT
     LSEFLAFLRN VQGEDVEGNR AAWEKSFYRH ARKYRPESTS EGLEDLISED AFVAFLSSRH
     NTPVADEPQD YTLDRPMNEY FISSSHNTYL LGRQVAGRSS IEGYIAALVR GCRCVEVDCW
     DGPDGQPQVV HGRTLTTSIS FKEVMTTINK YAFVKSNFPL WISLEVHCNA VQQAIMAETI
     KEAFGSRLVT EPLDPSSNKL PSPSELMGRI LIKVKEPRMH DDGNMSSAAV IAQATRGRGN
     SVGSSSQPAH VSESPAPYIS QSLPQSPLLS GYPRRVASNS RKRVQTINEE TTHVRDMSSN
     SDTESGSDTG SGSPSANKTI PVLGRLGVYC AGVKFPGFDT PAAKKFNHIF SFMESSFSKN
     SRSKEDKMSL NIHNMRYLMR VYPDGTRLAS SNFDPLIYWR RGVQMAALNW QTFDLGMQLN
     RAMFDGGQDS SGYVLKPPEL RDIQVLPYNS DIARGKKERS VVSFSVDMLS AQQLMRPANL
     SASKSMDFYV EVEVFHANDK RDKKEGHFDG DNGTDTPLKF QTEVIRENGF SPMFMSGQFK
     FKVVTKHPEL VFVRWSVKLS NDGESYSTKD RPPIASYTAK LRNLKEGFRT LPLLNHAGDQ
     YLFSTLFCRI QIDEIEKTLI DAPRSPSDGS KLNRFGGKVF GRSNTSPRGT IEKTNVEKTS
     FESYA
//
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