ID B9T6G8_RICCO Unreviewed; 635 AA.
AC B9T6G8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Nodulation receptor kinase, putative {ECO:0000313|EMBL:EEF28551.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EEF28551.1};
DE EC=2.7.11.26 {ECO:0000313|EMBL:EEF28551.1};
GN ORFNames=RCOM_0295930 {ECO:0000313|EMBL:EEF28551.1};
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).
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DR EMBL; EQ974608; EEF28551.1; -; Genomic_DNA.
DR RefSeq; XP_015583629.1; XM_015728143.1.
DR AlphaFoldDB; B9T6G8; -.
DR GeneID; 8284751; -.
DR eggNOG; ENOG502QT13; Eukaryota.
DR InParanoid; B9T6G8; -.
DR OrthoDB; 1215196at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
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; 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 PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR PANTHER; PTHR48010:SF59; OS07G0681100 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 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 Kinase {ECO:0000313|EMBL:EEF28551.1};
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 Oxidoreductase {ECO:0000313|EMBL:EEF28551.1};
KW Receptor {ECO:0000313|EMBL:EEF28551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EEF28551.1};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..635
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002890053"
FT TRANSMEM 255..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..635
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 635 AA; 69661 MW; F80E0932612B5601 CRC64;
MKFFPASSFR LIVLFTLFSL AIADLNSDKQ ALLNFSAAIP HYRLLNWNPA SSICKSWVGV
TCNPSQTRVL ELRLPGVGFI GQIPANTLGK LDALRVLSLR SNLLYGNLPS DVTSLPSLRN
LYLQHNNFSS TIPTSFSSQL NVLDLSFNSF SGSIPQTIAN LTQLTGLSLQ NNTLSGAIPD
LNQSRLRHLN LSYNHLNGSV PFSLQKFPNS SFTGNSLLCG LPLNPCSPIL SPPSPSPASS
PPPEMPHKKG SKAKLTLGAI IAIAVGGFAV LFLIVVIILC CCLKKKDNGG SSVLKGKAVS
SGRGEKPKEE FGSGVQEPEK NKLVFFEGCS YNFDLEDLLR ASAEVLGKGS YGTAYKAVLE
ESTTVVVKRL KEVVVGKREF EQQMEIVGRV GQHQNVVPLR AYYYSKDEKL LVYDYIQGGS
LSTLLHGNRQ AGRTPLDWDN RVKIALGTAR GIAHLHSAGG PKFTHGNIKS SNVLLNQDHD
GCISDFGLTP LMNVPATPSR SAGYRAPEVI ETRKHTHKSD VYSFGVLLLE MLTGKAPLQS
PSRDDMVDLP RWVQSVVREE WTAEVFDVEL MRYQNIEEEM VQMLQIGMAC VAKVPDMRPN
MDEVVRMIEE IRQSDSENRP SSEENKSKDS NVQTP
//
