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Database: UniProt
Entry: M4BMQ8_HYAAE
LinkDB: M4BMQ8_HYAAE
Original site: M4BMQ8_HYAAE 
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
//
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