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Database: UniProt
Entry: A0A0D9NXI1_METAN
LinkDB: A0A0D9NXI1_METAN
Original site: A0A0D9NXI1_METAN 
ID   A0A0D9NXI1_METAN        Unreviewed;       648 AA.
AC   A0A0D9NXI1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=H634G_06219 {ECO:0000313|EMBL:KJK78521.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK78521.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
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; KE384734; KJK78521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9NXI1; -.
DR   STRING; 1291518.A0A0D9NXI1; -.
DR   Proteomes; UP000054544; 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; 2.
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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          362..475
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          474..619
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          150..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   648 AA;  71491 MW;  6B2F6B0C9C127F2A CRC64;
     MAALQQAGGG ASQAQRAPPT LTNTVISYLK TIFESHADAD GRWTLGQIAR FIQQVQKNSD
     KTTAAAKLLQ STEIDLSAFL QYMTSEDSNI TEPWNQSDLS WPLSSYFISS SHNTYLSGNQ
     LYSDSTTDAY TNVLLRGCRC VEIDVWDGDE SDLSASSTES SADEKADDEA VPTKSKRHGT
     FDRLRQRIPD SLTSKLEKTS LAKTLELKHT GKHNTDTANG ALPDGDSKIV PEVALVEPRV
     LHGYTLTKEV SFRDVCNAIR DSAFTVSDLP LIISLEVHCG AEQQVMMANI MKQVWSGMLV
     TEDEIKPGLL PSPEDLKRKI LIKVKYAPPD TPAAEPDSSA EDDSSPAEAA PPKKPSKVVQ
     ALSKLGIYTR AVSFKTWTQP EASMPTHIFS LAEKKFIEHR EKHAQALFDH NRDYLLRAYP
     SGLRITSSNM MPTVFWGSGA QVVALNWQQT DEGMMLNEGM FAGTCGYVLK PEGYRPNLPS
     KPTPNKITYK TLNLSLTFLA AQSIPLPHGD KSDKRFHPYV KTELHVDACN APAHGRPGSS
     ESLDTDVRHK ARTKTHKGTD VDLGRQQVSF NGIDGLVEEL TFVRFTVRDD ELGRDDLAAW
     ACVRLDRLGQ GYRFIHLIDS KGHLTDGTIL VKVEKTLVEE KPDGKEGA
//
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