ID M4BMQ8_HYAAE Unreviewed; 963 AA.
AC M4BMQ8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=PI3K/PI4K catalytic domain-containing protein {ECO:0000259|PROSITE:PS50290};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP807695, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP807695}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP807695};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH598426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BMQ8; -.
DR STRING; 559515.M4BMQ8; -.
DR EnsemblProtists; HpaT807695; HpaP807695; HpaG807695.
DR VEuPathDB; FungiDB:HpaG807695; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_005963_0_0_1; -.
DR InParanoid; M4BMQ8; -.
DR OMA; YDKYQRW; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 668..948
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 592..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 108065 MW; 49891E0CC2B710B5 CRC64;
MGLFNLLALT VETSVLGVYV VVPLASSDGY TLLASDVRSV LQFHQSLALQ ALLSVLRLLL
FVYIRRRNKR VPSTRCFVFV VSLVEVVVCA LGSLQLLLYL DGKHVDTFSK YRRVSWGGLY
IIALGLMAVL STMLQLGYIL QLNKSRGRLS DDKLLRDVLG ETPRAKWRSK WATLGKQLAG
RQKHKDTTFE AMVRLYAHQD GAVDQLAASS DQDEGEFEFY LPQLCGFLLL GAFARSPQLY
AVLLRKSEYG AVPAVASAGP PSPTKSELYQ LGAGRESDGG ENSREDEALL PRLRDDHYAT
FEETHDIERG LASSAVPSMP RIPGTEPFEL ETAFLRSLAN VSSNLRAAAY NSRNDMLRVW
LQDLEAQYLP SNSLYLPVGN SYHRLKHIHV DESFTFSTRE RVPFLLCAEV VDYPSPQQEH
AARNKGHRSM FNGRRFTLGL WDAGTNPDVN SNCASAERTP LMSPDASKLG FWSESRILNS
PTRLRSFSHH ISNKMAQPTE LLHGLLDSLA GKNSGSKTYD SKDEALLSKV ESHEYDEDTT
SSFRNLPERC QSQPFFESLG AFSKQTERVH TSSPGLQVAA PTSVVPISTD VGVSDLESNG
SGPWSPHSDT SQSPQSESSA CSAHNLVRLD STDQFLQDLT ERDSKLEEAE RAEDTGLPSE
KCHPTMGGEP PCVIFKERWA DKERRIQATS PYGQLPGWRL LPVIVKSDDD LRQEQLALQL
IRQFAKVFEE FKVPVFIRPY DVIAISATSG LVEAISDTIS IDSLKRNDRE FTTLLNFFTR
HFGDPGTPGF HRARSNFVSS MAGYAIVCYL LQIKDRHNGN ILLDAEGHII HIDFGFILAN
NPGNMAFEQA PFKLTADFVE LMGGPRSAHF RRFRSLCVRS FLVARKYRHR FVLLVEMMLH
GNEHLPCFGG DPKYTVERLA ARFQPDLDIN SCEDFVHELI DASLDNWRTR WYDKYQRWIV
GVF
//