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Database: UniProt
Entry: R9NW48_PSEHS
LinkDB: R9NW48_PSEHS
Original site: R9NW48_PSEHS 
ID   R9NW48_PSEHS            Unreviewed;       588 AA.
AC   R9NW48;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   22-FEB-2023, entry version 43.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   ORFNames=PHSY_000279 {ECO:0000313|EMBL:GAC92724.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC92724.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
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; DF238767; GAC92724.1; -; Genomic_DNA.
DR   RefSeq; XP_012186311.1; XM_012330921.1.
DR   AlphaFoldDB; R9NW48; -.
DR   STRING; 1305764.R9NW48; -.
DR   GeneID; 24105590; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   HOGENOM; CLU_002738_3_1_1; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000014071; 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; 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:SF169; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 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; 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:UP000014071};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          317..434
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          429..569
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          26..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  64959 MW;  6D65FBFBCE44F6C5 CRC64;
     MSDNTDPNTK DGKAAPSVLT SKFAKLNPFS KTGASDPEGG GDNLGEEVEF DSIAGGGHAA
     RRTKITKSEL RVSHALRQFL VDEKLISPAD AQLDDPQASS SDALKALVDQ SHIDVPEYVR
     DRSRPLSEYF VSSSHNTYLL AHQLYGTSSA IAYEHVLVTG ARCVEIDAWD NDDDPQEPKV
     THGYTLASHI PFRAVCETMK QAIQKEEEEA QRDQSFKVAP VLLSLENHCG HAGQQRLVEI
     MHEVWGDLLI SGPVEKNEPA SEHTSVEHLG AKIAVMVEFH LSKEAPVAEA TEEDDAEEKL
     NKAKRNEAKK AGIIPELCAL GVYAQSVKPV NDSWYTSTLT NGPHDHLINI SETGLIDLLP
     KQATAIKKHN AQHLMRVYPK GTRISSKNLN PVPFWGVGAQ VCALNWQTFD HSVQLNEALF
     SGSDGYVLKP PGLRIDGDGN TSLGRHKLTL HIAGATDLPL PAGKDADEIR PYVTCTLILP
     SDLKSEPPKR KTNAYKQHKL GIIHKGEQPI PTDPLWNEQL EWDFEHDELA FLRILIKSDD
     KFARNPLFAV AAVRLVYAAQ GWKFIRLLDL KGRETHSTLL VKFDLQKL
//
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