ID B9RWM9_RICCO Unreviewed; 1145 AA.
AC B9RWM9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Leucine-rich repeat receptor protein kinase EXS, putative {ECO:0000313|EMBL:EEF44281.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EEF44281.1};
DE EC=2.7.10.1 {ECO:0000313|EMBL:EEF44281.1};
GN ORFNames=RCOM_1022390 {ECO:0000313|EMBL:EEF44281.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; EQ973823; EEF44281.1; -; Genomic_DNA.
DR RefSeq; XP_002518148.1; XM_002518102.2.
DR AlphaFoldDB; B9RWM9; -.
DR GeneID; 8265641; -.
DR KEGG; rcu:8265641; -.
DR eggNOG; ENOG502QQEU; Eukaryota.
DR InParanoid; B9RWM9; -.
DR OrthoDB; 460040at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 7.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27000; LEUCINE-RICH REPEAT RECEPTOR-LIKE PROTEIN KINASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR27000:SF758; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RGI1; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF44281.1};
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}; Oxidoreductase {ECO:0000313|EMBL:EEF44281.1};
KW Receptor {ECO:0000313|EMBL:EEF44281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF44281.1};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1145
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002891389"
FT TRANSMEM 727..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 787..1074
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1088..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 816
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1145 AA; 123970 MW; 35329397BF02034B CRC64;
MSMPSSRQIL FFSSSSSCLS FFILTLLSTS LASPPQQQNH EASILFSWLR SSPSPPSFLS
NWNNLDSTPC KWTSITCSLQ GFVTEINIQS VPLQLPVPLN LSSFRSLSKL VISDANLTGT
IPIDIGNSVS LTVLDLSSNS LVGTIPESIG QLQNLEDLIL NSNQLTGKIP TELSNCTSLK
NLLLFDNRLS GYIPTELGKL SSLEVLRAGG NKDIVGKIPD ELGDCSNLTV LGLADTRVSG
SLPVSFGKLS KLQTLSIYTT MLSGEIPADI GNCSELVNLF LYENSLSGSI PPEIGKLKKL
EQLLLWQNSL VGVIPEEIGN CTSLKMIDLS LNSLSGTIPS SIGSLVELEE FMISNNNVSG
SIPSDLSNAT NLLQLQLDTN QISGLIPPEL GMLSKLNVFF AWQNQLEGSI PFSLARCSNL
QALDLSHNSL TGSIPPGLFQ LQNLTKLLLI SNDISGSIPP EIGNCSSLVR LRLGNNRIAG
GIPKEIGHLR NLNFLDLSSN RLSGSVPDEI GSCTELQMID LSNNTVEGSL PNSLSSLSGL
QVLDISINQF SGQVPASFGR LLSLNKLILS RNSFSGAIPP SISLCSSLQL LDLASNELSG
SIPMELGRLE ALEIALNLSY NGLTGPIPPP ISALTKLSIL DLSHNKLEGD LSHLSGLDNL
VSLNVSYNNF TGYLPDNKLF RQLSPADLAG NQGLCSSLKD SCFLSDIGRT GLQRNGNDIR
QSRKLKLAIA LLITLTVAMV IMGTFAIIRA RRTIRDDDES VLGDSWPWQF TPFQKLNFSV
DQILRSLVDT NVIGKGCSGI VYRADMENGD VIAVKKLWPN TMATTNGCND EKSGVRDSFS
AEIKTLGSIR HKNIVRFLGC CWNRNTRLLM YDYMPNGSLG SLLHERTGNA LEWDLRYQIL
LGAAEGLAYL HHDCVPPIVH RDIKANNILI GLEFEPYIAD FGLAKLVDDG DFARSSNTVA
GSYGYIAPEY GYMMKITEKS DVYSYGVVVL EVLTGKQPID PTIPEGLHVA DWVRQKKGGI
EVLDPSLLSR PGPEIDEMMQ ALGIALLCVN SSPDERPTMK DVAAMLKEIK HEREEYAKVD
MLLKASPAAA ADTENKNSRN GVPATTSSSK PQQTMANLYP KSNNSSFSAS SLLYSSSRNA
KMGFK
//
