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Database: UniProt
Entry: A0A067SYQ3_GALM3
LinkDB: A0A067SYQ3_GALM3
Original site: A0A067SYQ3_GALM3 
ID   A0A067SYQ3_GALM3        Unreviewed;      1105 AA.
AC   A0A067SYQ3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=GALMADRAFT_157070 {ECO:0000313|EMBL:KDR75207.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR75207.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(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; KL142381; KDR75207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067SYQ3; -.
DR   STRING; 685588.A0A067SYQ3; -.
DR   HOGENOM; CLU_002738_1_2_1; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 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; 2.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
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; IPR002048; EF_hand_dom.
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; PF00168; C2; 2.
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; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027222};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          317..352
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          780..895
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          890..1080
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..734
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..977
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  123484 MW;  E02DA02E709C02C0 CRC64;
     MADPPTSTMN PARRLRRAQV VKEVADESPS MPGSPPPKTN GFGASIRRQF LKARSAVSRS
     KSLNGTGHPT HSTATSEAEE ETQKTRQKGH SRSLSDVSAA LPRSDVLVAP PNVPPPMESA
     QSHSERLPSV SECPPISLPT TAVVDLSSSP AIGNVRVPQL LQQGTPMTKV SLKKHKKFVF
     RLDADLGQIV WESKKHKIIP IENIKEIRSG DDARYYREQF QLSQDYQDRW LTLSYLLDGN
     YKTLHLIAAT TDVFRMWDRT LRELHAIRLE LMRGLGNVEM RQALWEKHYW KGADEESDQK
     LTFEEVEKLC RRLNINSNGE DLLRLFKQAD SQKHDFLDFD DFRRFVKLLK ARPEIDRLYK
     KLKADNNGVF DFGVFEKFMA EEQESSLSSS GLQKIFDKYS KLTIPTDHPE GPATCPESNL
     PSSSTIPAAT CPGKMTVDAF ASFLLSPDNS VFADQHKDTW QDMTRPLSEY FVSSSHNTYL
     VGHQLVGVST IEGYIRALLH SCRSVELDIY DGEQEPMIFH GKTFTSKVSL REVCQTVAKY
     GFVASPYPII ISAEVHCGLA GQEMIAEIMI KEFGDSLIRI PVDNGSSTIV RERIEQLPSP
     EDLKGKILLK AKNRNLARAD SVESDRTSST DPSSSASDSD ALFEMMKDVI HLPAHIEEKK
     ENDKEAEKKH RRQSESTVKD QLAKAGTNIM KRVKSVGKSA TMPAPLSLLS PSSPRPSTSF
     IQPQPLPPPT AIVPPSSAST TFSALSQGLK SPTSLSAGRT SDVSGNGDGR PPKPKMSFAL
     LALLVYTVGV KFRGINKKEE YAPEHIFSLS ENTANKMLRF GMWDLIKHTK THMVRTYPKG
     MRLSSTNYEP HRFWAAGAQL VAINWQTFDL GYMINHAMFQ RNGRSGYVLK PDAIRLAHKE
     RLAKRTMHSF DVTIISAQQL PRPRDASGHE VPEKAIVDPY VEVTLYVPDW PVVLDHKTKE
     KEREKEKGKD RVRHHQRPTT PTAAVAAAAA TVLPIAVPAA SPTPGHAVSS RTSVVRKNGW
     NPVWEEKLRI PFDCVGDMMD LIFVRFVVRQ EDKDAVEPLA VYCGSLGSLQ HGYRHLPLHD
     SQLSQYLFST LFVRINVTPI EPPPP
//
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