ID A0A084QG00_STAC4 Unreviewed; 1135 AA.
AC A0A084QG00;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=S40285_02253 {ECO:0000313|EMBL:KFA62885.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA62885.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA62885.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA62885.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL660774; KFA62885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QG00; -.
DR STRING; 1283841.A0A084QG00; -.
DR HOGENOM; CLU_002738_1_0_1; -.
DR InParanoid; A0A084QG00; -.
DR OMA; HWQREMS; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000028524; 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; 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; 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; 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:UP000028524};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 422..457
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 797..915
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 126616 MW; B50B3A6571705235 CRC64;
MTTVLTEPEP IHSSSPTSHP SMASKPASLR RSRPSHVQTN FQPHSPAAFP TSAISSSSRA
SNSQQGSPIM SPETAVLTTS SSIQASPEPL RSRDDDTCPP NFELPDPILS RKTSANSLGT
SIVSSPSAMA EAISSTNPTS ANNAAKGSII RRLSSRASRS LNRRRRQSSA APTSRDGSVG
PCFLRRRSDS NTTAPPDFAS LVTDSESDLD DLDDLSSLTS LVGLDGAVWE SSAGTPNSSM
PVSSSAMAGP VLPPHHQKGT WLRKVSKKSR TKRIFLVYET DTNKLTWDKS RPQKYLHVDE
IKEIRFGSDV HQYNSDYRIS EVERSRWFTI IYMAPEKSRT KFMHLIADDE ETYSTWTRFL
GSMLKHRQAS MISLMAFDDM AIAQFWRSEM SRQFGDQALS TDQQELDIVG VKRVCTNLHI
WSSESVLEEN FRLSDLRGRG RLNFHEFLGF VRRMNRRKEV QSIMMRTAAR PDLGLTLTEF
LGFLQDSQGE DVENNRSMWE KTFARFARRY RVEDLDAIDT GNEQLLSEAG FVGFLASKHN
SVIVEEPQEY TLDRPMNEYF ISSSHNTYLL GRQVAGQSSV EGYIAALVRG CRCVEVDCWD
GSNGEPMVVH GRTLTSSISF RAVITTINKY AFEATNFPLW ISLEVHCNAA QQAIMAATIK
EIFGAKLVTE PLDPNSDKLP SPSELMGRIL IKVKKARCKE EPTAGDSRGR RRGSSLSSPS
VQPTIPESNG PALSPSIPQS PLLTPSTSAR RLVAKSRVNT ITEGEVQELM SSSTSDNDSG
SDSSLKRKSD NKTVEVLGRL GVYCAGVKFS GFDTKDAKRF NHIFSFMESS FAKHSRSKEE
KMALDIHNMR YLMRVYPDGI RVNSSNFDPL LYWRRGVQMS ALNWQTFDLG MQLNQAMFQG
GTDSSGYVLK PAELRDIQVL PYNSDIARGK KERSVVSFSI DVISAQQLMR PANLAANKSM
DPYVEVEIFH PNDKRSKKEA QTGLMQEPDS PLKYQTEVVR ENGFNPVFND GQFKFKVTTK
HPELVFVRWS VRLATDRDGY KPPVASYTAK LKNLQQGYRT LPLHNHSGDQ YLFSTLFCKI
KVDSIEKKLI DVQPPVQDVS KLNRLGGKVF GRINSSPRGT METSSTEKSS FESHG
//
