(data stored in ACNUC7421 zone)

SWISSPROT: Q75C92_ASHGO

ID   Q75C92_ASHGO            Unreviewed;       877 AA.
AC   Q75C92;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=AGOS_ACR024W {ECO:0000313|EMBL:AAS51251.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51251.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51251.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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; AE016816; AAS51251.1; -; Genomic_DNA.
DR   RefSeq; NP_983427.1; NM_208780.1.
DR   STRING; 33169.AAS51251; -.
DR   EnsemblFungi; AAS51251; AAS51251; AGOS_ACR024W.
DR   GeneID; 4619552; -.
DR   KEGG; ago:AGOS_ACR024W; -.
DR   HOGENOM; HOG000115576; -.
DR   InParanoid; Q75C92; -.
DR   KO; K05857; -.
DR   OMA; VCQNLHI; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR   GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
DR   CDD; cd13360; PH_PLC_fungal; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR037755; Plc1_PH.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336; PTHR10336; 1.
DR   Pfam; PF09279; EF-hand_like; 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; SM00054; EFh; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
DR   PRODOM; Q75C92.
DR   SWISS-2DPAGE; Q75C92.
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU00448};
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:UP000000591};
KW   Transducer {ECO:0000256|SAAS:SAAS01019513}.
FT   DOMAIN          288..323
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          595..713
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   CA_BIND         301..312
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00448"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..571
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   877 AA;  100559 MW;  018B354E539BD8D5 CRC64;
     MDLNHAYKAS NGESNNSLDS SLDVKPMEKP ATDDAVRTEK RKYHGAAVMS HHQISVMSQP
     LTKGVRELIK KTTAFMSCSK SKPQKLMELG PMTYAHSVLT ASEKPLCHME LESSSVNGFA
     DTLQDNGVSD ATLVEMWLIR VTRRKRVRYC FRISNGVLTW KDNRMLELDT IKDIRMAEMA
     KNYREQYDIM DAFASRWITI IYQVSPTKLK ALHLIAPTQL ECAKFYNAVL TVARQRRELM
     ESISVPSSEA FANIHWKVNV SSKKADESRD TLSFEDVQRL CTKFHIYCSS NYLKRVFKIA
     DVNRNGLLNF SEFCTFVRML KKRHEVTEIW QKIAAETRAI DFEKFYSFLT DVQCEDMDAQ
     LARDLFNEYS HEGYMDEDLL LKFLTAQPYA REIEEDYSRP LSEYFISSSH NTYLLGNQVG
     SMASVEGYIQ ALQQGCRSVE IDIWDSDDGP VVCHGKLTSS LPLRNVVDVI NKYAFITSPY
     PLILSLEIHC RSEGQIIVKQ LFDDILGPLI YVADHSVGWP SLRDLKHKII IKSKKLRVNV
     DMAADIYHST SSKGSSYDSE YDVQSQPSSP MPRRGMRGIH ISKRKHRVIE QLLQISAIHG
     ITFRNFSLPE SKTPTHCFSL SERSFDNLAN DDLQRLAIDK HNRRHLMRVY PHAFRYKSSN
     YDPIKCWRLG VQMVATNWQT YDLGQQLNQA MFRVTARDDW PWPSGYVRKP EYLLHTVPKT
     SFIRDIYEAV HSSVVALSLE LLSAQLLPKP KLSSRDGEAH FAPYVVIEVL GDGLCGPIHV
     QNGLVTAPNQ VTSCRCPENG FNPVWKTSLT ATLNNTGFNF IRYIVKNADI TLATCCIRLD
     YMKRGYRHIP LYSLESSRFI FSTLFVKTDY RIVRSLF
//

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