ID A0A194V240_9PEZI Unreviewed; 1139 AA.
AC A0A194V240;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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=VP1G_05260 {ECO:0000313|EMBL:KUI57964.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI57964.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN714706; KUI57964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194V240; -.
DR STRING; 694573.A0A194V240; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000078576; 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; 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; 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:UP000078576};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 428..463
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 798..916
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 930..1074
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 127709 MW; BE10EAB6989CDD1E CRC64;
MSFTTQATQE PASSPSLLQE PTMPSQKPQT SQPSQLRRSR PSQVQTHNLT SQPQTTTAPH
SAFTNSSMAS SPQQVSPVLS PESEILTNNS SIQPSPEPTR GRDCESSPLP LIEPLPEPII
TRKTSTNSLP QSLSSERSTQ NEPVQPKKNI IRRISTRVKT ESSRLRGNRR TSSTHPVSRD
ASVGPAVLRR GRSDSSATAP PDYAVAIGSD SDDETGIARE QQVSHPVPIA EGEAVRDFSP
ASTAASVAAS SRSSDIHTGP VIPQTLLQGM MISKVSTKRR KRLNLVLDAE AGKVSWDKNR
PSKCVYIDDI KEIRVSPDVR QYRLDCGAAE AEETRFFSIL YAVPDKKQKT MHLIADDDDA
FQAWVTTLDA LAKHRQALMS SLMSFNDRAI RIYWRKEMAR LYSENPPVDE QIDFAGVERV
CRNLHIHVSQ ESLKAKFDEA DKTQTGQLNF DEFQDFVRLT ARRGDVRAVY REIASDPEGG
LTCEDFIKFL KHVQNENVED VASWEAVFHQ FSRVKQVEPS PAGCSSEKPR MSESALAKYL
TSIHNTPLEA VPKDCELDRP INEYFISSSH NTYLIGRQVG DVSSIEGYIS ALMRGCRCVE
VDCWDGPDNQ PIVTHGKTLT SQIQFREVIG AINKYAFVKS AYPLWISLEV HCNATQQEVM
ANIMKDIFGE KLVTDKLEGY EDRLPTPEQL KGRILIKCKT PNFNEPKNAE ANGTGRKRGN
SLTSPFSRPT TIPESPVPNS PLLGPNHPAV RRGSNRRVNT ITEGEISDAR EALSSSSSDD
SGPEKNRRSK QSKITKVLGD LGVYCLGIKF RGFDDADCKI FNHILSFKEG TFLNNSSTKA
SKGALFRHNM RYLMRVYPGQ YRFTSNNFDP LIYWRRGVQM AALNWQTFDL GMQFNQAMFA
GGKDASGYVL KPRAFREIEM IPNSLSRFET TPNYPEELNN KRERKNVTFT IDIISAQQLM
RPFNLGERRT VNPYVEVEVF LADDKRDKQE ANGQPLRGPL RHRTKIIKEN GFNPVFDNKF
TFNVKTKYPD LVFVRWSVKL SEGGNYNDRS PAVATYMAKL TSLKQGYRTL PLLDHNGDRY
LFSTLFCRIK VDPITSVFVD YDAVLDNSNK LKTLGRTVFA RTAGQSPKSS FEKDSGYTP
//
