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Database: UniProt
Entry: A0A0F8WVL1_9EURO
LinkDB: A0A0F8WVL1_9EURO
Original site: A0A0F8WVL1_9EURO 
ID   A0A0F8WVL1_9EURO        Unreviewed;       610 AA.
AC   A0A0F8WVL1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-JUN-2023, entry version 31.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=ARAM_003557 {ECO:0000313|EMBL:KKK15357.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK15357.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK15357.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK15357.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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:KKK15357.1}.
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DR   EMBL; JZBS01003327; KKK15357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8WVL1; -.
DR   STRING; 308745.A0A0F8WVL1; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000034291; 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; 1.
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; 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; 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:UP000034291};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          335..448
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          142..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  67069 MW;  7C90E0648CBDF1AA CRC64;
     MATVNELTEH AAHISLNSSS EAIPAFSPSF KTHLDQVYGS LTSSKQNLLK DIQHESPDQT
     LSGDPLSSLA AFHAYMASPA ASAMRPANPP DTSAPITDYF ISSSHNTYLT GNQLYSNAAA
     SAYTHVLLSG GRCVEIDVWD GERESEGDHD DDTSSSGESR LSSLSSKVGS IIHRKPAPRE
     VSSGQTNPAP SKPKLGCPEP RVLHGRTLTR STTFRKVCHA IRDSAFVTSD LPVIVSLEVH
     ACLEQQGAMV EIMEETFKDM LIQVTPEMEA METPPPLADL KRKILVKVKW VPATSGDQDE
     VDDHPDDSEP LSHTASANTT ASAGPKKSSK ILHALSRHAI FTKGFSFKQF TQPEAKIPGH
     VFSLSEKAAR QDDVKFENAF FEHNRKFFMR IYPSGLRVNS SNLDPTFFWR RGAQIVALNW
     QNSDKGMMLN RGMFAGEHGW VLKPQGFRST EPESAPIPRR KLDLTIEFLA GQDIALPPGD
     KSEKGFHPYV ACYLHVETPQ DSPAGSGGES STDSEKSSYK RVIKSSSGAN PEFNSQKIQF
     PPLFGIVEEL TFVRFKVKDD EIGRDSLAAW ACIRLDRLRE GYRVIRLCKC DGSESGGYLL
     VRVTKNISEI
//
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