ID I1J386_BRADI Unreviewed; 1057 AA.
AC I1J386;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=100833639 {ECO:0000313|EnsemblPlants:KQJ85237};
GN ORFNames=BRADI_5g25790v3 {ECO:0000313|EMBL:KQJ85237.1};
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:KQJ85237.1};
RN [1] {ECO:0000313|EMBL:KQJ85237.1, ECO:0000313|EnsemblPlants:KQJ85237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ85237.1,
RC ECO:0000313|EnsemblPlants:KQJ85237};
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:KQJ85237.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ85237.1};
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:KQJ85237}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ85237};
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; CM000884; KQJ85237.1; -; Genomic_DNA.
DR RefSeq; XP_003579462.1; XM_003579414.3.
DR AlphaFoldDB; I1J386; -.
DR STRING; 15368.I1J386; -.
DR EnsemblPlants; KQJ85237; KQJ85237; BRADI_5g25790v3.
DR GeneID; 100833639; -.
DR Gramene; KQJ85237; KQJ85237; BRADI_5g25790v3.
DR KEGG; bdi:100833639; -.
DR eggNOG; ENOG502QV5Y; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; I1J386; -.
DR OMA; WLDHIAE; -.
DR OrthoDB; 377080at2759; -.
DR Proteomes; UP000008810; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR45974:SF219; OSJNBB0004A17.8 PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 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; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1057
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014095727"
FT TRANSMEM 701..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 775..1046
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 803
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1057 AA; 113424 MW; 05ADC4C5A224828D CRC64;
MGGFFRLLLA VSVLLHVLVH GGGQLLLSLN QTCDAADLAA LRAFSNGLDG SPGAGQLAGW
DAPVSGSGSC CAWTGVTCDG LGRVIGLDLS NRSLHGVVSP SLASLRSLAE LNLSRNALRG
ELPTAALALL PALRVLDLSA NSLSGDFVPS SSGGAPNESS FFPAIEVLNV SYNGFTGRHP
SFPAAANLTV LDASGNGFSG AIDAAALCSG SGALRVLRLS ANAFSELRIP AGLGRCQALA
ELALDGNGLA GAIPADLYTL PELRKISLQE NSLTGNLDER LGNLSQLVQL DLSYNMFSGG
IPDLFGKLNK LESLNLASNG FNGTIPGSLS SCQMLKVVSL RNNSLSGVID IDFGSLPRLN
TLDVGTNKLS GAIPPGLALC AELRVLNLAR NKLEGEVPEN FKDLKSLSYL SLTGNGFTNL
SSALRVLQNL PKLTSLVLTK NFHGGETMPV DGINGFKSMQ VLVLANCALS GMIPPWLQTL
ESLNVLDISW NKLNGRIPPR LGNLNNLFYI DLSNNSFSGE LPESFTQMRS LISSNGSSER
ASTEDLPLFI KKNSTGKGLQ YNQVRSFPPS LILSNNLLAG PVLPGFGRLV KLHVLDLSCN
NFSGHIPDEL SNMSSLEVLN LAHNDLNGSI PSSLTKLNFL SEFDVSYNNL VGDVPTGGQF
STFATEDFVG NSALCLLRNA SCSQKAPVVG TAQHKKNRAS LVALGVGTAA AVILVLWSAY
VILSRIVRSR MHERNPKAVA NAEDSSGSAN SSLVLLFQNN KDLSIEDILK STNHFDQSYI
VGCGGFGLVY KSTLPDGRRV AIKRLSGDYS QIEREFQAEV ETLSRAQHKN LVLLQGYCKI
GNDRLLIYSY MENGSLDYWL HERADDGALL DWPKRLRIAR GSARGLAYLH LSCEPHILHR
DIKSSNILLD ENFEAHLADF GLARLICAYE THVTTDVVGT LGYIPPEYAQ SPVATYKGDI
YSFGIVLLEL LTGRRPVDMC RPKGSRDVVS WVLQMKKEDR ETEVFHPNVH DKANEGELIR
VLEMACLCVT AAPKSRPTSQ QLVAWLDDIA ENRSLAQ
//
