ID I1HID6_BRADI Unreviewed; 634 AA.
AC I1HID6;
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=100821199 {ECO:0000313|EnsemblPlants:KQK05730};
GN ORFNames=BRADI_2g22180v3 {ECO:0000313|EMBL:KQK05730.1};
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:KQK05730.1};
RN [1] {ECO:0000313|EMBL:KQK05730.1, ECO:0000313|EnsemblPlants:KQK05730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK05730.1,
RC ECO:0000313|EnsemblPlants:KQK05730};
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:KQK05730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK05730.1};
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:KQK05730}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK05730};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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DR EMBL; CM000881; KQK05730.1; -; Genomic_DNA.
DR RefSeq; XP_003568238.1; XM_003568190.3.
DR AlphaFoldDB; I1HID6; -.
DR EnsemblPlants; KQK05730; KQK05730; BRADI_2g22180v3.
DR GeneID; 100821199; -.
DR Gramene; KQK05730; KQK05730; BRADI_2g22180v3.
DR KEGG; bdi:100821199; -.
DR eggNOG; ENOG502QT13; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; I1HID6; -.
DR OMA; CESWVGI; -.
DR OrthoDB; 1215196at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR025875; Leu-rich_rpt_4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48010:SF88; OS05G0480400 PROTEIN; 1.
DR PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..634
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014094570"
FT TRANSMEM 254..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..610
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 634 AA; 69350 MW; 7068374998D9E1D0 CRC64;
MQHLRLIAFL SASLLFPLLP CTKGADLNSD KQALLAFAAS LPHGKKINWT RTTQVCTSWV
GVTCTPDGKR VRELRLPAIG LFGPIPSNIL GKLDALQVLS LRSNRLTVGL PPDVASIPSL
HSLYLQRNNL SGIIPTSLSS NLAFLDLSYN SFNGEIPLKV QNMTQLTGLL LQNNSLSGSI
PDLQLTKLRY LDLSNNNFSG PIPPFLQKFP VNSFLGNSFL CGFPLEPCPG TTPPSPVSPS
DKNNKNGFWN HTTIMIIIIA GGGVLLLILI IILLICIFKR KRDTEAGTAS SSSKGKGVAG
GRAEKSKQEF SSGVQEAERN KLVFYDGCSY NFDLEDLLRA SAEVLGKGSY GTTYKAVLED
GTTVVVKRLK EVVAGKKDFE QQMEIIDRLG QDQSVVPLRA FYYSKDEKLL VYDYVLAGSL
SAALHGNKSA GRTPLDWGAR VKISLGAARG IAHLHAEGGK FIHGNIKSNN ILLSQELSAC
VSEFGLAQLM ATPHIPPRLV GYRAPEVLET KKPTQKSDVY SFGVLLLEML TGKAPLRSPG
RDDSIEHLPR WVQSVVREEW TSEVFDVDLL RHPNTEDEMV QMLQVAMACV AVAPDQRPRM
EEVVRRIEEI GSSYSGTART SPEDKPKEEA IQMT
//
