ID M4B9E7_HYAAE Unreviewed; 3272 AA.
AC M4B9E7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:HpaP802906, 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:HpaP802906}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP802906};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; JH598031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 559515.M4B9E7; -.
DR EnsemblProtists; HpaT802906; HpaP802906; HpaG802906.
DR VEuPathDB; FungiDB:HpaG802906; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_0_1; -.
DR InParanoid; M4B9E7; -.
DR OMA; MRQHSAK; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 2.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1655..2373
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2548..2864
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3240..3272
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1242..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2850..3044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3108..3157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1726..1753
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1259..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2850..2870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2871..2900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2919..2950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3108..3145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3272 AA; 359479 MW; 316BDA75037AD978 CRC64;
MQFQDREHVE HTLLVSLVQR LDVPDAATRH ARVAELYAAV TSLHRQLSAE RFAKALGQVT
PQLYKLLQKG ASESAHLGAL LAIERLLDVS NEDQFIRFVN YLRYFVQQPQ TSSTALLAAA
SAMGYLAASR VSGTLVASFV DFEAKRAFEW LQEAAGGAHA QRHEALVSQR RLAACFILRE
LAQAAPTLFH VNLTLFFQSI WGAVRDARVE IRDAATSALA ACLQLITRRQ TRHRVQWYCK
VYDQVVKGLA VRPRSKASAN ALVASPDQTV LATWECAHGS LLVIGELLAN TGRFMVPRFR
EVCDTVLQYK DAKERLVNRA VSRLLPQLAE FCPGAFVQYY LDVCVAHLTK KILEYSAPAA
ERGVSFLATG RLALAVGDAL LPHLPPILKL VRESLAPHTG SKRKRARNKL FCVQTLTCVA
NMSRALGSQF EPFLFQYGVL ETMMIGGLSD ELIDALAEVV ASVPSALPYV QERLLNEISV
ILRGTPFSLG SNGAVYASCS SGVTSSSPDG NRSELTLDAS YYDTPSEALP VKQTAVQALL
SSMKRGFSSA EDDSTSGNGS LMIKGETGDE IDTILLSLRT LSCFDFSGSF CLLPFVRDCV
ALYLKNPDAR IRKQAVITCS KLLLPSPESP DTALMSSWRH VKKRGLSGRV IDHVLTQLLQ
VGISDMDVAV RRSVVESLDA RFDELLSQEA HLKLMFLLLN DENAKIRECA MQLLERLAPR
NPAFTMPSLR RLVIQLVTEL QHTSDLRMRE DSTRLLGHLV RSAQHLVDPY VVRILEVLLP
ILVRGNASLT VAVLITLGEL ALVSRTQIAA YERYLFPLII HTLQDHSSTE KRQVALQTLG
QLAGSTGCVI RPYLASPKLL EIFLSLLHHN VGSPWSLRRE AMRTIGILGA LDPYKYKLCI
SRASLRQANE VASTADTSTA ADRDEKKVGR ATLSVSNSIS DTRMSQYPTL NIDQKALGLT
IDLASFDRKA TSDALDEKQQ AELQLFTAAP IGTRKVDAGT ATGTLGVGLQ SSYPANGTAA
ASDGAPLSSL SSSCRRKREV VSIGMSRSDD TFDFESSLVD NELELDPTEL SPASDAYFPT
VAIHALLHIL REPSLNAHHH GVIQAIMFIF KSLSTQCVSF LKYILPPFLR VLARGEPRLR
ESLFLQLTTL ISIVNAHMKP FFPPIMALAL RFWGSHLPQI VRLVEEISQA APHEFHTQYF
PKVLPKLLEV LQPHFGLGNG ASDGNLSGAT AGGAATIPQS FGDGAGGAGG GGDNHAQGRG
NVSGGNSDHT SSTYDIVQNG GADGSVVAAI QVQVVQSLIV FGDAVSDYVY LLVPALVHLM
ESLDTPLEVK ITTIYALARI SVVASFEQYA GPRLLQPLAR VASQISAKGP FFFSRSSSSV
SSSGVSGGST ASTLSGSSAG AVAAQIATTK TEAIRFSEVM LYALGALVFQ LQGEILSYEP
LLQQIITSLP FSYHGSLTTA TNAPESSNSA SRPQAMVLRI AQALEHVRCG RRVPLSFLDD
RVFMTPTLRK FSTDVQAQTA ASMTPAASLP TNVRLHVNQQ NLQRAWEASQ RSTKEDWLEW
MRRFSIELLR ESPSAALRSC CALAQAYNPL ARALFNPAFV SCWNELYEQY QDYLVRALET
AFQSDTIPAE ILQTLLSLAE FMEHDVEALP IDIRELGELA QKCHVYAKAL HYKELEFHTS
PSTCIEALIS INNQLGQPEA AVGILKYAQA HHSRVIQVKE TWFEKLQDWR AALALYNRRL
QNAQAQGESE SEQGLDIEVC IGKMRCLEAL GEWEELSALA AQVWSFLRSP ERTSTKTIAV
PSRGRLLSAG LAPTSSSGVG SGTSDPALMR RGSSSSLGSS TNLAAAGGPP SSSSYQSGDD
RCDEDTALKR VAMLGARASW CLSQWDNMTQ YVTECAAQND SNSAVIFKAA NGTVHGNGYG
HTHGYGIFGA DEDVTELSLY QSILAVHQGN FVRAEVLIDA TRKTLDTKLG ALVGKSYSRA
YRSMVTLQQL SELEEVVMYK KLRAQISKGE EAARYKRHLM CMWRDRLSGC KRVVEVWQQL
IAVRALIVAP HEDIDTYLQF ASLCRQSGNL SLSLKVFTNA LHVYGGAGSS SAGISEMLRM
APPSSGSVST FGFGEKDRNR VAFAYLKHLW AAGQKQEALS DLHHLVIRIS ATARQRSQAT
SGLSGMSSTA PAMLPLKNEG EELLVKCHLK MAEWQLAIHD QQIEHVPVES VLSSLRLCTE
LDPRNYKAWH AWALMNFQVV EHSTHSQHIS ANATASAVTA SASVAPYIAP AIEGFFRSVA
LGRSRWAANV QQDILRVLTL WFAHGHRTDV HGALEKGFRS VSIETWLIVI PQLIARIHTP
SLRIQNQLYR LLVAVGKQHP HALIYPLSVA LKSSVCERQQ AAEAIMSTMR TNYVELVDEA
LLVSRELIRV AILWHEMWHE GLEEASRLYF GEHNVDGMAE VLRPLHAMME RGPETLREVS
FHGAFGRDLR EANEWLQRFL SNRRNESDLN RAWDLYYHVF RRINKQLPQI TTLELQVVSP
NLLSARNLQL AVPGTYRAGH SIVKIGSFLP TVAVITSKQR PRRITIVGSN GLEYMFLLKG
HEDLRQDERV TQLFGLVNAL LVNDRNTSKK DLKIHRYPVI PLSDNAGIVG WVPHCDTLHQ
LIRDYREARK ILLNIEHRLM LQMAPDYDAL TLLEKVEVFQ YALENTAGQD LYKVLWLKSE
NSEVWLDRRT NYTRSLAVMS MVGYILGLGD RHPSNLMLHR FTGTIVHIDF GDCFEVAMDR
EKYPEKIPFR LTRMLTNAME VSGIEGNFRF SCESVMAVLR ENRHSLMAML EAFVHDPLIN
WRLLSASNML SSSHVSSSIA SSVVSSSIMS SMSSQSDGGM YEPSEASSHD TSDVSSHDET
EMSSHDPGEE KARHRRSESI SIPDPTPASM AALLDEGNEP RLTSSSRVQC TQKVSARGPN
EMQDTNKLSA EARGDTVAVK ERDADDSDGE PSDDTSDPAA QQQPLPRGKP PVPRQGGANL
ADPRQLPPRP EAKGVEAVPP PLPSSLSSRP MSLSKSIPLP VRKLPPRVPA TNRVHEDAID
ENEEFNVVEK IDYSTTNLNV EISSLAASVS SVGHSSLSRS FSVTQAQMQA QSRATEQQAR
QQQQQRRQEN CQAARLDTER QSVAPSTPAG PPPRIVPAAS TSFVSVTAAA QIPPASDAAS
PSMINELHAS RSIRERELLS ALGPEGIAAP RVALNEKAVA VIRRVQAKLS GRDFEGDGGE
PLDVSAQVQR LISQATSHEN LCQCYIGWCP FW
//
