ID A0A1S9DQD8_ASPOZ Unreviewed; 1145 AA.
AC A0A1S9DQD8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=OAory_01077510 {ECO:0000313|EMBL:OOO11281.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO11281.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO11281.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO11281.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OOO11281.1}.
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DR EMBL; MKZY01000003; OOO11281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DQD8; -.
DR VEuPathDB; FungiDB:AO090012000557; -.
DR eggNOG; KOG0169; Eukaryota.
DR Proteomes; UP000190312; 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; cd16207; EFh_ScPlc1p_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; 1.
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; 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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 2.
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:UP000190312};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 403..438
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 781..899
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 894..1057
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 127190 MW; 8EC5965B16B21BDD CRC64;
MAYAATSSAS TVNGDARSSL KLTASSSNPP KLHHVITSIP PAPNPSSAPS YTSSLTTTPN
SLRPAYFPSN ASSPSGTPLQ IATDGLRGRI PPFPAIPSTT FELGESVMAV LGNAPASGSG
DAVISNSKGP GLMRRISRGA ANKLTRRRQS ASHNEKRDRS SGPVTMRRRS DSKTGSQNGR
DNALESSNEE DSNDALDSLG VWCGSESSSL PNESFMAASR HTGTIAPKID SAIQRGTVLT
KVTKKRRKQV RFFLDLDAGK VYWDVSNPAK RFYIDDIKEI RVGVDARNYR EEHQIPQDTE
NRWFTIVIAD DERSKGRTVK TLHLIAPNTP ILELWTTTLE HISRYRIGLM AGLAGSGQSE
AVLKAHWQRE MSRLFPHGTR SAEQGSLDFG AVESICRSLH INCSKNMLRA QFSKADSDVN
GKLNFSQFQN FVARLKERKD VKEIFKDSAT DAKAGLSVDE FLKFLRNIQN ENVDSDRSYW
VSVFDKCVRK SKSRVPSIPE FEEEQVPRMD LDAFSSFLAS PWNGLYASRA PQSRFDRPLN
EYFISSSHNT YLLGRQVAGA SSTEAYISAL QKGCRCVEID CWDGADGRPI VSHGRTMTTS
VLFADCITVI NRYAFITTDF PLILSLEVHC NPEQQLAMVK IMKDTFKDQL VLEPLLTNSF
VLPSPEELKG RILVKVKTCD ELQEGVRQEP VGTFAVHGRK RSASSPFIRP TASESSAITS
LPPLSSPPTL GLETVGSFLT QDRRSFTTTS ISSAAEESDG ALATIRKEKK RRQKSKITKP
LSDLGVYTRG YKWHSFSSAE SQRYNHVYSF AERSFEGICR DAENKALFEK HNRKYLTRVY
PSGFRLRSSN FDPLKFWRRG VQMAALNWQT YDIGMQMNQA MFAAGSDRTG YVLKPESLRA
LCPADEEKTK TTEWKLVRFS VDVISAQQLP RPRSIGPDDN INPYVEIEMF SADDRGQSFV
YGEGGMNASA RNGMSGIGFP HRRRTKIEQS NGYSPIFNDR FRLSLETKYP DLVFVRWTIW
SSQDGRSAGS NSSVQLATFT AKLSSLSQGY RYLPLYDGGG DQYLFSTLFC KITKEDPVSV
QRLDAEELRA ERMGILRQIG QTVFKRTSST ERERGNDMAT SAEDKDSSPD LTPTVSAAST
SSLPP
//
