ID J3LKP6_ORYBR Unreviewed; 726 AA.
AC J3LKP6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=102712786 {ECO:0000313|EnsemblPlants:OB03G16220.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G16220.1};
RN [1] {ECO:0000313|EnsemblPlants:OB03G16220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G16220.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB03G16220.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
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DR RefSeq; XP_006649512.2; XM_006649449.2.
DR AlphaFoldDB; J3LKP6; -.
DR EnsemblPlants; OB03G16220.1; OB03G16220.1; OB03G16220.
DR GeneID; 102712786; -.
DR Gramene; OB03G16220.1; OB03G16220.1; OB03G16220.
DR KEGG; obr:102712786; -.
DR eggNOG; ENOG502QRHD; Eukaryota.
DR HOGENOM; CLU_000288_92_2_1; -.
DR OMA; ETTNDYM; -.
DR OrthoDB; 466261at2759; -.
DR Proteomes; UP000006038; Chromosome 3.
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; 1.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF39; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000006038};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..726
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003773990"
FT TRANSMEM 298..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 425..699
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 253..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 726 AA; 79395 MW; DBF90B7CBC00A9E5 CRC64;
MGRRGRGGGM ADAPWLPLLL LLGCFCSIWP QRQILVAADT DPNDVTVLNT LFTSLNSPGQ
LKGWQASGGD PCGQSWQGIT CSGSSVTAIK LSSLGLSGNL AYNMNTMGSL IEIDMSQNNL
GGGQQIQYNL PTSKLERLNL AGNQFTGNLP YSIFSMNNLK YLNLNHNQLQ GNITDVFSSL
YSLTTLDLSF NSLTGDLPQG FTSLSSLKKL YLQNNQFTGY INVLANLPLD DLNVANNRFT
GWIPSQLKKI NSLQTDGNSW STGPAPPPPP YTAPPPPNRP NSPGQNNGDS SSGGSSGIGG
GGVAGIVISL LVVGAVVAFF VIRRRKRKAA MEEHFEQHQP FTSFPSNEVK DVADMKPIEE
SATIDIESLP SPASISLKPP PKIERHKSFD DDDLSNKPVM KKTNVPPIKA DVYSVADLQM
ATDSFNMDNL VGEGTFGRVY RAQFTDGKVL AVKKLDSTVM PFHSSDDFAE LASDISKLHH
PNLNELVGYC MEHGQHLLVY DFHRNGSLHD LLHLSDEYSK PLSWNSRVKI ALGSARALEY
LHEICCPSII HKNFKSSNIL LDSEFNPHLS DAGLASFISD AEFQAAQQSA GCTAPEVDMT
GQYTLKSDVY SFGVVMLELL TGRRPFDSTK PRPEQSLVRW ATPQLHDIDA LDRMVDPALK
GLYPAKSLSR FADVLALCVQ PEPEFRPPMS EVVQALVRLV QRANMTKRML DGDSSRRADD
QDQDFI
//
