ID A0A2K2D692_BRADI Unreviewed; 2270 AA.
AC A0A2K2D692;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=100845900 {ECO:0000313|EnsemblPlants:PNT69799};
GN ORFNames=BRADI_2g00627v3 {ECO:0000313|EMBL:PNT69799.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT69799.1};
RN [1] {ECO:0000313|EMBL:PNT69799.1, ECO:0000313|EnsemblPlants:PNT69799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT69799.1,
RC ECO:0000313|EnsemblPlants:PNT69799};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT69799.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT69799.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT69799}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT69799};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM000881; PNT69799.1; -; Genomic_DNA.
DR EnsemblPlants; PNT69799; PNT69799; BRADI_2g00627v3.
DR Gramene; PNT69799; PNT69799; BRADI_2g00627v3.
DR Proteomes; UP000008810; Chromosome 2.
DR ExpressionAtlas; A0A2K2D692; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
DR InterPro; IPR003152; FATC_dom.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1149..1808
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1914..2226
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2238..2270
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1111..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1670..1697
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1114..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2270 AA; 255738 MW; 5AC60D236A53CA66 CRC64;
MVIKKHDELS HGLTSLGSAF ETTGSVLSSF QSFLSSPIFR LRRVSNKVSS VLIKDVTGLL
DELLVAFSQL FSRLSSSLNT SDSESTGKIL PISSVNLLED LNHVVGHKSS VLDMDFDVTD
SGEVDSITAS VSGSIGISSR PLEWKLELVC VISTFFSVSP PHAWEILYSL VEKEIDVKVC
QAILLNLCQN ISASPKSLSS LVHLISNTRE KCESSLLGSA DCLTHVHALL RTLIATRDVG
QNTDGKPQAC NMVSNENQDT LLDLVTKGTE ISITDWFFRI KLIDCISHFI YLFPDIAQDM
TGHLLNMLHD TDYRVRLYLA RKIVVPFQIW EGHNELFHDV CSNIGVKMVQ FSNKIAVKSR
EVLAAGPQSV PVIETVLITL AHLSVHSEEV EVECAFMISA AAAIETSQRE LAYALFDSVS
RTLSYASRNK YLDQLTGPIL FRWVACEMSL VSLVEVQEIF GFNSSESKNF IEHICSWLLS
FLILRGDAAD LNWISKILSQ PLSAVIKGYF VPIFGLSIAA RCGTGPEKDL AETVLYDSLL
QFGEISESER DDLIRKHMVS IVGLLLSVSS TAHQPEFPYF SREILAFSIK TVVDGFVDTT
DDDLADTVVV DKINIFRADR VFKFLLAIHQ QVADASHPRH MGHRLCAIEV LIDVLGHRVV
HYSTCFYIIC IVGNYIWRQP LQGQCCNILT KLLTAFNASP TTETVSALGM QLQLLVPKLV
TCCLSNDKER RNGNGDSSKV LSLLRQLTVD ADPLLYDYIR DLEPLPALDC LKDIHVFHAS
LSDSYASRDQ FLKFVNRAPH LPAELFLLSL RMHHKKLLLG EIICRGDASV GNADTVSCWH
SDPDVVSAVW TLVDLCSSSS VANEASSVLA DFISRAGISD AHQVIFHVPN LTQKHSSQLQ
SGSTSKDDKL CSDYGISDDI LVGLLKLLKT YLSDDSVEII DVTSQTLRGI LSTSKGVNSL
QCLDSLDKSL LMVHSRGINI QLVEQTLLGL EKYSAGSLED SDIWQTDGRS YDQWLCTLVS
SLICHCDDII LRLCRSLVFL KVEAAELLLA SALVNIAGNV DSNNSICGLI SSKVEKIIFC
DSNHLMKSVN LFLDALNVVR SFYVAEKTRD CPSNTPKVGR SARSKSRSPA ATPSSSWKKV
YWLSVDYLVA ARAANRCSCD FATLMYVELW CEEQFNKLAL GPPDFSQDES LPAHMGLLVA
AFTHINEPDS IYGITLANEI TSQIIRYEHE GDWSSALEYY DLLVRSTPKE NLGNFAGTVL
AGPSAVFSKA EEKNWKMHKG LMRSLQKTGC SHVLDFYSQG LTNQKTCLQQ DSEFIDIQYE
AAWRAGNWDF SFFIPYSSQP SSRSRNYCLF NENLHSCLRA LQSGDFEQFH GKLSHSKMDL
VLALSNASKE STKYIHSTVL KLQMLDHLTM VWDLRWKIYH NETPKSYVGT DEFSPIPAVP
TRNQLEFLNK EWNFILCQTE RNLDLFEPFL AFRRTLLKIL GCEEHLIDHL FQSASALRKG
LRFSLAAASL YELKELCCHR DQQTMANTYF LSKLEEAKLL RAQGQHDMAI GLGKYILQNH
TDKKDITDVY RLVGKWLAET RSSNSRTIIE DYLKHSVDLT EFHKSPDKKY MSRQCRTYFH
LAHYTDNLFK SYEERLSSNE WQAALRLRKY KTRELDTLIK RFKSSSKGEK TDYSVKIQEL
QKQLALDKEE AQKIQDDRDR FLSLALQGYQ RSLVVGGKYD LQVVFRLVSM WFSLFSREQV
VKSMIKTTKE VQTYKFIPLV YQIASRLGSS KDAQGATNFQ NALASLLKKM AIDHPYHTIF
QLLALANGDR VKDKQRSRSS FVVDMDKKLA AENLLKELSS FHGALIRQMK QMVEIYIKLA
ELETKKEDTN KKIPLPRELR NICQLELVPV VTATVPVDPD CRYEEGTFPH FSGLLDSVMV
MNGINAPKVI ECIGSDGNKY RQLAKSGNDD LRQDAVMEQF FGLVNMFLQN HRDTSERRLR
IRTYKVVPFT PSAGVVEWVN GTVPLGEYLL GSNRNGGAHA RYGTGDWTFL QSREYLTCEK
DKRKAFLKIC DNYRPVMHHF FFERFLQPAD WFQSRLAYTR SVAASSMVGY IVGLGDRHAM
NILIDQDTAE VVHIDLGVAF EQGLMLKTPE RVPFRLTRDI IDGMGITGIE GVFRRCCEKT
LSVMRENKEA LLTIIEVFIH DPLYKWALSP LKALQRQKET VDTDSCLEDS QEACEGNKDA
ARAILRVKQK LDGYEDGEMR SVEGQVRQLI QDAVDVDRLC QMFPGWGPWL
//
