ID A0A179UCV1_BLAGS Unreviewed; 1153 AA.
AC A0A179UCV1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BDBG_00914 {ECO:0000313|EMBL:OAT04342.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT04342.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; GG657449; OAT04342.1; -; Genomic_DNA.
DR RefSeq; XP_002628006.1; XM_002627960.1.
DR AlphaFoldDB; A0A179UCV1; -.
DR STRING; 559298.A0A179UCV1; -.
DR GeneID; 8507076; -.
DR KEGG; bgh:BDBG_00914; -.
DR VEuPathDB; FungiDB:BDBG_00914; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000002038; 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; 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; 2.
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; 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:UP000002038};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 404..439
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 773..891
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 895..1054
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 129170 MW; 1B55667FFFA7A70E CRC64;
MASGGWPSPS TLKDNSHSRL NSSPSQGPRR IPFQDVLSSS TLSSTAPSVS GFGPSGPSKS
SPGLPAHFSS APSPSTFSLN GSADSSRDPA VRNTFSPTFA LGSPLPLELP ESVMAFPTYP
NAPPSGIDGI GNNATSNKAP GLMRRLSRGT ANKLSRRRQS TSHHDKRDNS SGPVIMRRRS
DSKTGTTTSR DSGLDSSYEE EEEGCGTWCK PETNSTTNGY NMSGTATHTC TAPELDLILH
RGSPLTKVTK HKRKRVTFFL DLHAAKVYWD LSNPAKRLYI DDIKEIRTGL DARNYREEHD
IPENLENLWF TIIFTNPEQS KNKPIKTMHL IAPNEATLEL WTNILDDISR YRIGLMAGLA
GTQSDTVLKA HWQREISRRV LEPGEESLDR NAIEALCQSL HINCSKNMLR AQITKADTEG
KGRLNFAQFK DFLQRLRDRK DIREIFRSVA ADPVQGLTLD EFLHFLREVQ RENVEENRNY
WCSTFESFSR NSKQRPEPRN SPDSRMDLDA FSAFLISPKN SVHLIRYSPP KFDRPLNEYF
ISSSHNTYLL GRQVVGESST EAYITALQNG CRCVEIDCWD GADGRPTVSH GHTMTKSVLF
ADCINVINRY AFQASEYPLI LSLEVHCSPI QQLAMVEIMK ETFGDKLVLQ PLLTNCPILP
SPDDLKHRIL IKVKTADEEE LLTSSHTHTT GRKRSSSSPF IRHTLPESNS ISMPFSQTSH
SVDAGSLPSW TAGRRSLTTT SISSASEDSD VGQLLTSTRK EKRRQKSRIT RELAELGVYS
RGYKFHSFNS PESKRFNHVY SFAEKAFERL CGDSESKALL EAHNRSFITR VYPSKFRVRS
SNFDPNSFWR RGVQMVAMNW QTYDVGMQMN QAMFASGSDQ TGYVLKPDSL RTSPSPRYIA
LSCDSKPKVD RKLVTFTVDI ISAQQLPRLK GMGPDDSINP YVEIELFCAD DKKKGLAFGE
GGVNTSARNG MSGIGQPHRR RTKIEQQNGY NPVFNDQFKL SLETKYPDLV FVRWVVRNSP
DGRSFGGNNS VQPATFTAKL SSLLQGYRYL PLYDASGDQY LFSTLFCKIT KFDPVPVRRA
GFEGWRGDQK GIIRQIRHTL SKRTSPTERD KERDSDRDRG KGKDAPQKSE DSHPRNKRSS
STDSSSCTIP SLP
//
