ID A0A175W5B6_9PEZI Unreviewed; 1101 AA.
AC A0A175W5B6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=MMYC01_205862 {ECO:0000313|EMBL:KXX78689.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX78689.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX78689.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-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 -!- 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:KXX78689.1}.
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DR EMBL; LCTW02000111; KXX78689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175W5B6; -.
DR STRING; 100816.A0A175W5B6; -.
DR VEuPathDB; FungiDB:MMYC01_205862; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000078237; Unassembled WGS sequence.
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; 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; 2.
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; 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; PF00168; C2; 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; 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; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 770..884
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 888..1039
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 122738 MW; FE28DFD42AC7AA4F CRC64;
MASEPAPLRR SRPSQVKTDL CTEPRLVAAP PSVISMSSVS PSSRDGSPVQ SAGTGPGTAS
SLQHSPESLE PEDTESQVTP FQLPEAIQIK PTDLTGFNLS RRTSTASLAQ GSLKSPGTTA
MGEAVKMSIV RRASNSVRNK AVGLLNRRPS STKPRSRDGS VGPGVMRRRG STSNPNTPFE
NISPFETDSD DDFGIGSDDL FGADKFCREP GSSSPAAAPT AYGSIPLALR QGMALTKVTK
KKSTKRITLC LDPDSAKISW DRNRSAKSIY IDDIKEIRIA EDIRQYRLDA GLPESSERRF
FSVIYSPLGK PGTKVLHLIA DDDEAFRQWI QGLETICKHR QHFAASLMSF NDKAIRTYWE
MEMDKKFGNK PRVERMCRCL HIHVSADELR RKFDTVKGRR ASSDDLPSSQ RYSSRLNFDE
FLEFVQLMKS RGDVRSAYQS YTADGEAGMS KNEFFRFLRD AQRENVDEDL AHWDGVFLRY
ARKGKPKDTE KMTGVGDDGF AMSEAAFASF LTSSSNEAIL KEPKSYVLDR PLNEYYISSS
HNTYLLGRQV AGISSVEGYI SALMRGCRCV EVDCWDGQDG QPVVMHGHTL TTRISFVEVI
KTINKYAFVK SRFPLFISLE VRCSPATQVI MANIMMEVFG DKLVKEPLDP SSDRLPSPSD
LMERIIIKVK RSQQPEESPR NGERPGRRRG NSLPSPYLRA VAADNLAGPV PASPLLSPTS
IPRPSRQINT IAEGVVHESL SSSGPSEYDS ESEKDSVSTK KVTSKINPIL GDLGVYCSGI
NFDGFESPEA KTFNHIFSFK EKTFAEKNQP GAGKRALYRH NMRYMMRVYP NGGRITSSNF
DPLVYWKRGV QMAALNWQTF DVGMQLNQAM FDGGTDNSGY VLKPLEGRQI QLMPNLSPDE
CVGKRRRKKV GFGIEIISAQ QLMRPWSLGE KRTLDPYVEV EVFLADDKRN KPESGAAPPA
QDAQLKYRTK IVRDNGFNPD FNQSFVFDVT TKYPDLIFVR WSVKLADSKG YNDKAPPLAT
FTAKLSSLKQ GYRTIPLLDN HGDRFLFSTL FCRIRKDQVT DIMVSYQEDV PKNGNKLKTI
SRTVFNPSTT SPKSSMDSFR S
//
