ID D0N7Q2_PHYIT Unreviewed; 1373 AA.
AC D0N7Q2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Phosphatidylinositol kinase {ECO:0000313|EMBL:EEY53601.1};
GN ORFNames=PITG_07286 {ECO:0000313|EMBL:EEY53601.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY53601.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; DS028127; EEY53601.1; -; Genomic_DNA.
DR RefSeq; XP_002905219.1; XM_002905173.1.
DR STRING; 403677.D0N7Q2; -.
DR EnsemblProtists; PITG_07286T0; PITG_07286T0; PITG_07286.
DR GeneID; 9471616; -.
DR KEGG; pif:PITG_07286; -.
DR VEuPathDB; FungiDB:PITG_07286; -.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_261661_0_0_1; -.
DR InParanoid; D0N7Q2; -.
DR OMA; MFQLQEV; -.
DR OrthoDB; 71507at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00891; PI3Kc; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR035448; PI3Kc.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEY53601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 168..275
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 280..378
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 461..630
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 656..770
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 830..1008
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1081..1358
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 155944 MW; 1FE999D180BA7489 CRC64;
MFSLNPRQSM QSVLQSSGSS SSSMRNTATS FISAAYSGYE GGASFRNVDA GLVPSFEALN
PYAKAGHSMM GDDKRWQPVP DLFHSKESLY FRSAVGKVLK TAHEEISPAE LEVRANTPEF
KVEEGDWIAH NSNQKNQFAL ITPLKTVARI PANLIISDEP ISLTQHMSNH MGGYLRKKGE
KNKAFKKRYM ELNGSVLAYY KKKPEKNGIP LSRDEKKSLE RGRIDLDRVS SLQPMESRSE
PYGILLVTTT RTWAICADSE PEYQRWLKGL CDVVKFSAVH VTYKRMFQLQ EVSAKAITDV
RMVVTTGDTV GQIVEHIFNC YEQALDAAPL RPYNPAEYRL KITGYRDYMI DRFRVLNEYV
HVRECLLTKK TIRLTVIHES VIQETALMNL SIGRDLPVST GSMNNIVSQF ADMFDGERAT
SLQMTTLGDE WERPSIDRNA SLPSGIIQQP FAICVRRVLN IPRTTCVRKR SSEEAIVTRI
PLTSSSVVVR IELYDGGQLL DNAVIDTSDV RLKAQRNDLL YAEWDDPVWH KFNIDICNVT
RTMRVQLTVL GVKKVVGGST SNMDATEEKM LVTGVNAFEV DDVLVQGHQY VHMYNNLHSC
VQGPVPHVTL PNEPMIQLEF SKFDAPIKFD WSDDDDSSES DRSYRRSIIT SSRSVMLRKE
GWLQKVGNFS SLTRWRRRWF VVDQSTCTLS YADDETAPRK LITLRNCSVM TADDMNQKFT
TAPVNKGTRK LRQTWCFKVR PMGSSRDYII SAETKQDREE WMLAIQTVAK GDTSISDFGS
HNGSFDDLIT PSVAESPRVE ESSEQLNGRN ILESVAQDRR DSVSRGSRSS GHSSYQREGE
LNELRKLILL DPLYRFSPYQ KEQLWMHREE FIDIPSALPR ILSCVHWDDR DECEEALTLL
PRWSVPDHQA AYIELLNGEF AHEGVRTFAV QKLSQMADTT FSYFLPQLVQ AIKFENHHVS
PLAMLLIERA IKNPNQIGFD LFWSMKVEAH NDQYRERYGT ILNAYLDVCS SKMRAILKLQ
DKLFSEGGML ERICQSVKAK RKDGAAEMKR AMQQGLEALN ELLPGSFQLP LDPRIEVGKI
IVSKCRVMDS AKKPLWLVFE NAEEGGDPVT VMFKAGDDVR QDCLTLQLIR LMDEMWRDEG
LDLAMEPYKC VATSPMTGIL QMVPNSVTTA EVHRRDGMMG TFKDPSFSDW IRANNSDPRS
HKAAVDLFGR SCAGYCVATC VLGIGDRHND NIMIASSGRY FHIDFGHFLG HLKYYKLGIR
RERTPFVFTN EMAYVLGGVE GKDFAKFVDT ACTAYCVLRR QMHLLVSLLL LMVPADMPEL
TGRDDINHIV TTLAPEVSDE RARESFEQTI HFCLDSRFKR FDNYLHNIAH AFG
//
