ID A0A2I1HEJ4_9GLOM Unreviewed; 852 AA.
AC A0A2I1HEJ4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=RhiirA4_331271 {ECO:0000313|EMBL:PKY57284.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY57284.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY57284.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY57284.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-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:PKY57284.1}.
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DR EMBL; LLXI01002496; PKY57284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1HEJ4; -.
DR VEuPathDB; FungiDB:FUN_008770; -.
DR VEuPathDB; FungiDB:GLOIN_2v1523224; -.
DR VEuPathDB; FungiDB:RhiirA1_343719; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000234323; 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; cd08558; PI-PLCc_eukaryota; 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; 1.
DR Pfam; PF13499; EF-hand_7; 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; 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:UP000234323};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 287..322
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 593..708
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 704..831
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 31..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 97791 MW; 0945968184E48668 CRC64;
MNTQPLISSA STLHHAYTFP LDKSSYRELD GRNSSIQNTT SDSNRKSVVI SDEKVKNSSK
VNTSPSTNIN TTFNNNALQI TSTKIITSID NEPAKKEINK IKPHILSRSI PVSSSPVEFH
SPDDILVDPC IARGTILYKV SAKKKQRRTF RIDVDQGRIL WDSKKSGKVN IENIKELRIG
EAIRNIRIHA KIGKEFEDRW FTIIYVEAGK YKSLHLLAES ADLFNKWVDN LQRLYLHRKD
MIGGLGHLRK RQSIWLKQHW KQANKDGDSK LVFDEVSRLC RQLNINMSRQ SLKAKFGEAD
TQNNGWLDFT DFQRFVKIIK KRPELDNLFE SLAKTKKDIL TLQEFKDFLL IVQKCNLKED
YDNLYYKFCD KDLNEMSLEG FNSFLMSSDN SVFASDHAKL YQDMTHPLCH YFIDSSHNTY
LLGHQLTGES SIEGYIRVLQ RGCRCVEIDC WDGPDGPIVT HGHTWTSKIL FQDAISAIRT
YAFKASPYPL ILSLEVHCSI EQQEHMAKIL SEILGEHLVT KFFSDDESEL PSPDSLMYKI
LLKGKNLPHG TAEDLFDSAT DTESATDPES DVESKDNADK KHKKGKSKVA KALSDLVVYC
SAVKFKGFDN SRNSKFYHMS SFSERVATRL TKTDKQSFIQ HNSRHLSRIY PSGYRIASSN
YEPQHQWMVG SQLVALNWQT FDLGMQINQA MFSVNGRCGY VLKPENMRNF ELTTTTNPLT
QYTLEVEIIS AQQLTGPKDL FKEIIDPYVE VELLMPGADV IKKKTKTVLD NGFNPIWNET
LTFTIDFEYL ELVFLRFTVW DEDVRLNEFI GYYCIPVASL QQGYRHIPLN DANGEQYLFT
TLFVRLSLKP II
//
