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Database: UniProt
Entry: A0A3N4LN15_9PEZI
LinkDB: A0A3N4LN15_9PEZI
Original site: A0A3N4LN15_9PEZI 
ID   A0A3N4LN15_9PEZI        Unreviewed;       960 AA.
AC   A0A3N4LN15;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=L211DRAFT_785303 {ECO:0000313|EMBL:RPB24274.1};
OS   Terfezia boudieri ATCC MYA-4762.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pezizaceae; Terfezia.
OX   NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB24274.1, ECO:0000313|Proteomes:UP000267821};
RN   [1] {ECO:0000313|EMBL:RPB24274.1, ECO:0000313|Proteomes:UP000267821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB24274.1,
RC   ECO:0000313|Proteomes:UP000267821};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(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};
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DR   EMBL; ML121542; RPB24274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4LN15; -.
DR   STRING; 1051890.A0A3N4LN15; -.
DR   InParanoid; A0A3N4LN15; -.
DR   Proteomes; UP000267821; 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; 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:UP000267821};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          274..309
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          630..748
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          755..912
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  108054 MW;  CA9142B2B9CF030B CRC64;
     MSEVYNQASG QKPGLMRRLS RGAANKLRKK TSSKGEEEKS GPLTMRHRNN SVSMNDLGLK
     HDSRSDDDDD YSISTAIVSS ADRAKDTLAG KPPNSAPPIS STSAGVVIPQ ALQRGTSLTR
     VTRKKIAKRT FKLDIQSAKV TWDPSKPSSR FFVDDVKEIR VGADARNYRE EFSISGDMEE
     LWFTIIYAEH EENGKLKALH LIAPDKESFT LWTSTLDKVL KYRTEFMSGL AVQGDKFVSE
     HWRNEFAAKS SPNKEEKLSF DRVERLCRRL HVNCSRRFLR QKFNVADVDK TGYLNFVQFQ
     KFVFLLKERV EIVELWKQVV RDEEGGMTRD EFWLFLLDVQ MVDVEADAIH IERVFRKFCR
     KSRRIERMTG LPSPVEPKDA ESRMSMEAFS IFLRSQAFNP PLLTTIAEKD LERPLNEYFI
     SSSHNTYLLG RQVVGESSIE AYIKVLQRGC RCVEVDCWDG DDGRPVVYHG RTFTTKVLFS
     DVIAAIGKYS FLVSPYPVII SLEVHCGLEQ QNRMAEILRS TLGEHLVSEP LISHSMVLPS
     PKDLKHKILV KVKSSEVQDI GMALSDIEVI KDISLHRPAR SSTIPQSPSG SGSSEGTSDS
     LDSDSHVSLP SGEVNVKKPK KKPKKIAPAL GQLGVYTRGQ KFSNFALPES KTYNHIFSFA
     ERTAMKFSKD PDKKVALEKH NTRYLMRVYP SGYRVNSSNF DPNTFWRRGV QMVALNWQTY
     DLGLQMNEAM FASLHDHTGY VLKPRELRIS RTTSDPLADA AAAKLRKDRK LVKFSIDVIS
     AQQLPRPKDQ KPDDSFDPFV EVEVFSADDK AKGASTVEGG IEAGDSKAAS GLGAPTRRRT
     TVVRENGFSP IFSTNGGGKM SFSIQTKFES LIFVRFSLYN DGHSGDRSSM FGSYTAKLTS
     LQQGYRHLPL YDNQGEQFLF STLFVKIKVD PIQPLDIIPE RSTALGSFRT GVKSVLGFSK
//
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