ID A0A0F7S3I3_9BASI Unreviewed; 1471 AA.
AC A0A0F7S3I3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 Name=SSCI75690.1 {ECO:0000313|EMBL:CDS01819.1};
GN ORFNames=SPSC_06491 {ECO:0000313|EMBL:CDU26297.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDS01819.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDU26297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU26297.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDS01819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-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};
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DR EMBL; CCFA01004619; CDS01819.1; -; Genomic_DNA.
DR EMBL; LK056694; CDU26297.1; -; Genomic_DNA.
DR STRING; 49012.A0A0F7S3I3; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000242770; 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; cd13360; PH_PLC_fungal; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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; 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; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 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}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 444..479
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 980..1101
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1471 AA; 159669 MW; CF74392B894AF195 CRC64;
MSANDQHTAV DRTANHSVRS WLRSLLRRPS DHTADVGEAG PSSGSAVVSP AGTDMISFHH
TMEDMDRPSF APPSRSFSGG SSNGALSYDA AARRTLAQPI ATPTLGASHA PHGLSPHASL
ATPPSPSASP PKSPGFGRTL SSSVASFTGR LHHQRRASET YRRMRSGSTS TAADSQQDGL
SRSLSRTLDV NAPLVASPPA LSEKEAAPNL SSVHLSYGSQ PSTTTQESRK LPASSDSKQS
NLPSTESQRS DPNSVSNAIS ASLPPVHSPN GAAAPANETV NELLLPEGEQ MLKVTHKKVK
PRTFKLDADR GQILWESKKN NRVNLESIRQ VRFGPSAASY RTSLNISSAH EPRWLTIIYQ
NGGIYKALHL IALSDSSLSR WRASLLHLQS LRRELTGAVG ASSSIEHRRH LWMRHHWKDA
DQSNDEKLSI EEVMLLCRRL GIESNKAHLR RCFNLADWRN RGYLDFQDFQ HFVSLLKQRA
DVQAIFAAWA DQPSDQHRRD SLTKTSTADE PEAEQALKLD GTSGVETTSE PATSLRQTTA
TTGPEPCRTR AISIENFRRF IREEQGNRTF TDGQIDDLFR RHCNSRLSTS HVADAPIEKA
RMDYDGFLDF LSSSDNPPLL DQLPVFSTMV SDPVDMPVLG KPATLTPPDS AQVGDSQPRL
QQHNSDPNPS RQQRTPSRAF ADTTEELIAA GASDSMANTR KIAAHLRKST VQHDMTRPLS
EYYISSSHNT YLVGGQWKGD STVEGYIRAL LQGARSVELD CWDGPNNVPQ ITHGRTLTSR
VPFQEVISAI ARYAFVTSPY PLILSLEVHA DPPQQDVMAR ILRDTLGEML LSQPLDSQQV
PGADDELPSP EKLKFKVLVK AKNVAAADSQ RVLHSKKSAD GLGLASQQKD GTDAVPTMVL
EPPTSATDTT ITTDSEIESR LAGAKELVRR VTRRGHRAEA AANGPSGYRS GDASEGIDVT
QREANRSSSK QAKKTMSTAL ASLLIYTIGV KCRGFNKKET YAIQHMVSLS EKTSLKMIRD
PISNEALIKH NRSHLTRIYP SMMSFARLHA SRNFIPLDMW ATGCQLVALN WQTTDLGFEL
NQAMFSRNGR CGYVLKPAAL RTKEHGKTRA DKAVRFRLDL NIVSAQQLPK KSKAGTGKDK
DKNGNNDTRE PIDPFVVVSL LAPACWGKQP RGLLQKASAK ESAVISLQPV EQGDAASAPA
AQVEPTDTPG RSELGRSDAT TSTEPARQSV DPTVLADASP ADKQGTETTA PKASTLAPSH
LLRTPTVKGN GFSPEWHTDM SVLIDVPAGA SDELLSLIEA SKASSQSGDA LAHPELERLS
RGLLDLCFVR FEIFDDDLDD HGVDGIATTK RAPDAKSIQS STSATSITDA TSRLSTDSTL
VNSKPSSVEA EIIGGTRSRA GSETSSASST SSIDAESVAA YSVSVGALQQ GYRHLPLYDH
QLSQFLFSTL FVRSRLRLVG LVDAVGRGKH A
//
