ID A0A015JTD1_RHIIW Unreviewed; 1054 AA.
AC A0A015JTD1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=RirG_271300 {ECO:0000313|EMBL:EXX50381.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX50381.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX50381.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) 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:EXX50381.1}.
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DR EMBL; JEMT01029976; EXX50381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015JTD1; -.
DR STRING; 1432141.A0A015JTD1; -.
DR HOGENOM; CLU_002738_1_2_1; -.
DR OMA; HWQREMS; -.
DR Proteomes; UP000022910; 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:UP000022910};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 489..524
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 795..910
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 906..1033
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 760..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 120442 MW; 50E779294C073219 CRC64;
MFACAVLAVS VLRKKCSKKQ KSNNKVINIK SDFPGGKQDL ETPEISFKPE KDTLEHLHKM
EQSNKSLVRD KSISQSVKLD AFENNFHHAD ARIDSNVSGS KEPSLRSNFS HTIGQNNRVD
NEVVSNISQV TNLMKNKAKI INSETGDADD SFNLTYLSIN NFNHFAKTAD TSSSDMIQSK
DTINSFVDSQ HLTRSHSDID FSMNTQPLIS SASTLHHAYT FPLDKSSYRE LDDRNSSIQN
TTSDSNRKSV VISDEKVKNS SKVNTSLSTN INTTFNNNAL QITSTKIITS IDNEPAKKEI
NKIKPHILSR SIPVSSSPVE FHSPDDILVD PCIARGTILY KVSAKKKQRR TFRIDVDQGR
ILWDSKKSGK VNIENIKELR IGEAIRNIRI HAKIGKEFED RWFTIIYVEA GKYKSLHLLA
ETADLFNKWV DNLQRLYLHR KDMIGGLGHL RKRQSIWLKQ HWKQANKDGD SKLVFDEVSR
LCRQLNINMS RQSLKAKFGE ADTQNNGWLD FTDFQRFVKI IKKRPELDNL FESLAKTKKD
ILTLQEFKDF LLIVQKCNLK EDYDNLYYKF CDKDLNEMSL EGFNSFLMSS DNSVFASDHA
KLYQDMTHPL CHYFIDSSHN TYLLGHQLTG ESSIEGYIRV LQRGCRCVEI DCWDGPDGPI
VTHGHTWTSK ILFQDAISAI RTYAFKASPY PLILSLEVHC SIEQQEHMAK ILSEILGEHL
VTKFFSDDES ELPSPDSLMY KILLKGKNLP HGTAEDLFDS ATDTESATDP ESDVESKDNA
DKKHKKGKSK VAKALSDLVV YCSAVKFKGF DNSRNSKFYH MSSFSERVAT RLTKTDKQSF
IQHNSRHLSR IYPSGYRIAS SNYEPQHQWM VGSQLVALNW QTFDLGMQIN QAMFSVNGRC
GYVLKPENMR NFELTTTTNP LTQYTLEVEI ISAQQLTGPK DLFKEIIDPY VEVELLMPGA
DVIKKKTKTV LDNGFNPIWN ETLTFTIDFE YLELVFLRFT VWDEDVRLNE FIGYYCIPVA
SLQQGYRHIP LNDANGEQYL FTTLFVRLSL KPII
//
