ID A1D7Q8_NEOFI Unreviewed; 649 AA.
AC A1D7Q8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=NFIA_069230 {ECO:0000313|EMBL:EAW21752.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21752.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21752.1; -; Genomic_DNA.
DR RefSeq; XP_001263649.1; XM_001263648.1.
DR AlphaFoldDB; A1D7Q8; -.
DR STRING; 331117.A1D7Q8; -.
DR EnsemblFungi; EAW21752; EAW21752; NFIA_069230.
DR GeneID; 4590295; -.
DR KEGG; nfi:NFIA_069230; -.
DR VEuPathDB; FungiDB:NFIA_069230; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_0_1; -.
DR OMA; SSYRRCT; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000006702; 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; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF82; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 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:UP000006702};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 375..488
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 484..630
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 147..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 70455 MW; 133408859E266AC1 CRC64;
METMEELTGR AATISLESAK PARSIQAQPG PLSSHLDKIY ASLTSTSTAD FIKDVQKEEI
AGSVEAGNPL ASLAAFRAYM ASPASDALCP AKGEDLSAPI TDYYVSSSHN TYLTGNQLYS
DAAAAAYTNV LLSGCRCVEI DVWDGDADDD SVSGDDTSSS SSSESNSDEE NPSRRKKQDV
PKTDGSTQST KAASRRKGLS SKLGSLLGRK SSPPNGATDK PASTATAAAV DAAQTLRRPE
PRVLHGHTLT KGTKFRDVCY AIRDSAFVAS DLPVIVSLEV HTCIEQQATM VEIMEEAFKG
MLIEVTPELE ATQAPPPLES LKRKILIKVK WVPATGDGQA EAQKDDQTDT LDTPPSVNQE
GQPAPAKPSK VLHSLSRLAV FTKGFSFRQF TQPEAKVPGH VFSLSESAAR EAYAKDRDAL
LEHNRHFFMR VYPYGLRVNS SNPDPTFFWR CGAQIVALNW QNLDKGMMLN RGMFTGEPGW
VLKPQGYRSS DPPSTPVKRQ QLDLSIEILA GQNLPLPPGD TKESGFRPYV SCYLHVECPD
EENGFPPGGD NTTDSEKTSY KRSIKSATGR NPDFGAQMIQ FPTLQGVIEE LTFVRFKVKD
DELGRDSLAA WACLKLSRLQ QGYRLIHLHD CSGAEAGAVL LVRITKVLS
//
