ID I1HDR5_BRADI Unreviewed; 1000 AA.
AC I1HDR5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=100836856 {ECO:0000313|EnsemblPlants:KQK03517};
GN ORFNames=BRADI_2g08350v3 {ECO:0000313|EMBL:KQK03517.1};
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|EnsemblPlants:KQK03517};
RN [1] {ECO:0000313|EMBL:KQK03517.1, ECO:0000313|EnsemblPlants:KQK03517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK03517.1,
RC ECO:0000313|EnsemblPlants:KQK03517};
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:KQK03517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK03517.1};
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:KQK03517}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK03517};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM000881; KQK03517.1; -; Genomic_DNA.
DR RefSeq; XP_003566237.1; XM_003566189.3.
DR AlphaFoldDB; I1HDR5; -.
DR STRING; 15368.I1HDR5; -.
DR EnsemblPlants; KQK03517; KQK03517; BRADI_2g08350v3.
DR GeneID; 100836856; -.
DR Gramene; KQK03517; KQK03517; BRADI_2g08350v3.
DR KEGG; bdi:100836856; -.
DR eggNOG; ENOG502QQFB; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; I1HDR5; -.
DR OMA; FKYRTFK; -.
DR OrthoDB; 391466at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1000
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014094501"
FT TRANSMEM 629..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 689..989
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 976..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1000 AA; 107220 MW; EFC46D68B2E0F45C CRC64;
MGAFLPILLL AAVAANAGLL LAQALNQDGL YLLDAKRALT VPAGALADWN SRDATPCNWT
GVSCDAAGAV TGLSLPGANI NGSFPAALCR VPRLQSLDLS NNYIGPDMAS EAVAGCKALA
RLDLSVNSLV GTLPGALAGL PELVYLNLEG NNFSGPIPDS FGRFPKLESL SLVYNLLGGE
VPSFFGAVPT LRELNLSYNP FAPGPVPAEL GDLAALRVLW LAGCNLVGHI PASLGRLRNL
TDLDLSTNAL TGPIPPEITG LASAVQIELY NNSLSGAIPK GFGKLAELRS IDIAMNRLDG
AIPDDLFDAP KLETVHLYSN SLTGPVPESA AKAPSLVELR LFTNRLNGTL PSDLGKNTPL
VCLDLSDNSI SGEIPRGICD RGELEELLML DNALTGRIPE GLGRCHRLRR VRLSNNRLDG
DVPGAVWGLP HIALLELNGN RLTGEISPVI AGAANLSKLV ISNNRLSGSI PSEIGSAAKL
YEFSADGNML SGPLPSSLGS LAELGRLVLR NNSLSGQLLR GFHSWKKLSE LNLADNSFTG
GIPPELGDLP VLNYLDLSGN RLSGEVPIQL ENLKLNQFNV SNNQLSGQLP PQYATEAYRS
SFVGNPGLCG EITGLCATSQ GRTGNHSGFV WMMRSIFIFA AVVLVAGIAW FYWRYRTFNK
ARLSADRSKW TLTSFHKLSF SEYDILDCLD EDNVIGSGAS GKVYKAVLGN GEIVAVKKLW
GGALKKDMEN SGEGSAADNS FEAEVRTLGK IRHKNIVKLL CCCTHNDCKL LVYEYMPNGS
LGDVLHSSKA GLLDWPTRYK VALDAAEGLS YLHQDCVPAI VHRDVKSNNI LLDAEFGACV
ADFGVAKVLE ATDRAPKSMS VIAGSCGYIA PEYAYTLRVN EKSDIYSFGV VLLELVTGKP
PVDPEFGEKD LVKWVCSTID QKGVEPVLDS KLDMTFKEEI SRVLNIGLMC ASSLPINRPA
MRRVVKMLQE VRAEERQRLE KDGKLSPYYY EDSSDQGSSV
//
