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Database: UniProt
Entry: A0A365N8Z7_GIBIN
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ID   A0A365N8Z7_GIBIN        Unreviewed;       579 AA.
AC   A0A365N8Z7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   22-FEB-2023, entry version 12.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=BFJ72_g1069 {ECO:0000313|EMBL:RKL49610.1}, FPRO05_02027
GN   {ECO:0000313|EMBL:RBA17303.1};
OS   Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA17303.1, ECO:0000313|Proteomes:UP000251714};
RN   [1] {ECO:0000313|EMBL:RBA17303.1, ECO:0000313|Proteomes:UP000251714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA17303.1,
RC   ECO:0000313|Proteomes:UP000251714};
RA   Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA   Sreenivasaprasada S.;
RT   "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT   strain ITEM 2341 from Date Palm.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RKL49610.1, ECO:0000313|Proteomes:UP000283569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fp_A8 {ECO:0000313|EMBL:RKL49610.1,
RC   ECO:0000313|Proteomes:UP000283569};
RX   PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA   Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA   Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT   "Characterisation of pathogen-specific regions and novel effector
RT   candidates in Fusarium oxysporum f. sp. cepae.";
RL   Sci. Rep. 8:13530-13530(2018).
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:RBA17303.1}.
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DR   EMBL; PKMI01000017; RBA17303.1; -; Genomic_DNA.
DR   EMBL; MRDB01000002; RKL49610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365N8Z7; -.
DR   VEuPathDB; FungiDB:FPRN_02316; -.
DR   Proteomes; UP000251714; Unassembled WGS sequence.
DR   Proteomes; UP000283569; 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; 1.
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:SF169; 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; 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; 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}.
FT   DOMAIN          306..424
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  65003 MW;  E3851B01E206E2F2 CRC64;
     MTSELATRIG DLNPFSSKSR RINDEDFGEE IDNNTVAGGG HSARRMVTDL RVSSALRDFL
     VKEKMLSKKE AKIDSQDSSR ELLELVSKPH IRVPPELTDR SHPLPEYFIS SSHNTYLMAH
     QLYGSSCATA YESAIRTGAR CVEIDAWDNS DDRDEPKVTH GYTLVSNISF RLVCETIRNS
     ADQEAVDAQK YGFRASPILL SLENHCDAYG QMRLVNIMRD VFGDRLLSQA VRHIGHEEQA
     GSGQHVKLED LGAKIAVIVE YHFTDEPSSS DSSSDDSEDE EEEKAARKEY KDKRKKEEPS
     IIIPELAELG VYAQSVKPMD NSWFEEGSLA NGPHHHLINV SESGLASHLP EHASHIARHN
     AHHLMRVYPK GTRISSTNLK PVPYWGIGAQ ICALNLQNFG TSNQLNEALF SGTDGYVLKP
     AALRAGGNGR LSTGRSKRLR LHVAGATDIP LHGDSEADSI KPYLTCTLYH PDNIKGDPPK
     RKTEPYKQHK LEFLHRGPNP PPTEPLWDET LTWEYEDNEL TFLRMLIKSD DSWTRNPMFA
     VAAVRLLYVE PGWRFIRMLD LKGHETQCSV LVNFEIIDA
//
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