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Database: UniProt
Entry: W9XW99_9EURO
LinkDB: W9XW99_9EURO
Original site: W9XW99_9EURO 
ID   W9XW99_9EURO            Unreviewed;       591 AA.
AC   W9XW99;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=A1O3_07566 {ECO:0000313|EMBL:EXJ81276.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ81276.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ81276.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ81276.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) 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};
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:EXJ81276.1}.
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DR   EMBL; AMGY01000006; EXJ81276.1; -; Genomic_DNA.
DR   RefSeq; XP_007735864.1; XM_007737674.1.
DR   AlphaFoldDB; W9XW99; -.
DR   STRING; 1182542.W9XW99; -.
DR   GeneID; 19171664; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   HOGENOM; CLU_002738_3_1_1; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000019478; 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   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:SF169; 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; 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:UP000019478}.
FT   DOMAIN          318..436
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  65259 MW;  1C35DA7F39D9BF7E CRC64;
     MAESGPSVLS SRLASLNPFS RPKSKTDGDD LGEKIDSSTV AGGGHGSRRS AITRDQLRVS
     HALRSFLVHE NVLSKNDAGL HDLGHLTDPL RALLGKPHIH VPSDLTDRSH PLPEYFISSS
     HNTYLMAHQL YGTSSAKAYE IALNTGSRCV EIDAWDDEDA EDEPKVTHGY TLVSRISFRS
     VCETIRDAVD REAALSASGS GYRTSPVLVS LENHCGNHGQ RRLVEIMKEV WDDRLLSKAV
     RGKGHREQNG SGDHVLLEEL GSKIVVIVEY HFPTEVEADD HSSSTDDEVD EDDEARQARK
     AYKEKKKAVP ATTIIPELAE LGVYAQSVKP ADNSWFGEVG LKNRPHHHLI NISETALRAH
     MPAEIGKIAQ HNAHHLMRVY PKGTRISSNN LNPVIFWGLG AQICALNWQT FGAGLQLNEA
     LFGGTEGYVL KPAALRAGGS GKLTTGPKKR LRLHVAGASD VPLPEGRQAS DIKPYLSCTL
     IRPDDQGQNP AKRKTALYKH HKLGFLHDGE NPAATDPVWE ETLEWEYEDN ELVFLRMLIK
     SDDSYSRNPV FAVAAVRILY VAAGWSFIRM LDLRGRETTC SLLVRFEVED V
//
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