ID A0A229XPX0_9EURO Unreviewed; 646 AA.
AC A0A229XPX0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=CDV55_108656 {ECO:0000313|EMBL:RHZ71540.1}, CFD26_104411
GN {ECO:0000313|EMBL:RLM00599.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ71540.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00599.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ71540.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RHZ71540.1}.
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DR EMBL; NKHV02000020; RHZ71540.1; -; Genomic_DNA.
DR EMBL; NIDN02000013; RLM00599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229XPX0; -.
DR STRING; 1245748.A0A229XPX0; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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; 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; 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:UP000215289};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 372..485
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 484..627
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 150..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70179 MW; 596200512C01BAB0 CRC64;
METMTELTGR TGSISLEAPK AARSGSIQIL PGPLSSHLDK IYTSLTARSP SDFIKDVQHE
EIAGNLEAAN PLASLAAFRA YMASPASDAL CPAKGQDLSA PITDYYISSS HNTYLTGNQL
YSDAAAAAYT KVLLSGCRCV EIDVWDGDAD TDSVSGDDAS SSSSDEGEKT SHRKKQDVSK
TDGSTQSTKK TSRRKGISSK LGSLLGRKSS PHDGASDNPA STATAAALDA ATQILRRPEP
RVLHGHTLTK GTTFRNVCYA IRDSAFVASD LPVIVSLEVH ACIEQQATMV EIMEEAWKGM
LIEVTPELEA TQAPPPLETL KRKILIKVKW VPATGDEAQK DDQTDALDTP PSLDRDGQPA
PAKKTSKVLH SLSRLAVFTK GYSFRQFTQP EAKVPGHVFS LSENAAREAY AKDRDALLEH
NRRFFMRVYP YGLRVNSSNP DPTFFWRCGA QIVALNWQNL DKGMMLNRGM FTGEPGWVLK
PQGYRGSDPP STRVKRQQLD LSIEILAGQN LPLPPGDTKA SGFRPYVSVY LHVESPDEEN
GSPPGGDNTT DSEKTSYKRS IKSATGTNPD FRAQTIQFPT LPGVIDELTF VRFKVKDDEL
GRDSLAAWAC LKLSRLQQGY RLIHLDDCSG AGAGAVLLVR ITKVLS
//
