ID B9STF3_RICCO Unreviewed; 851 AA.
AC B9STF3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=RCOM_1318870 {ECO:0000313|EMBL:EEF33104.1};
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; EQ974129; EEF33104.1; -; Genomic_DNA.
DR AlphaFoldDB; B9STF3; -.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR InParanoid; B9STF3; -.
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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF614; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF33104.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Oxidoreductase {ECO:0000313|EMBL:EEF33104.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
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};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..851
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002889630"
FT DOMAIN 537..840
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 851 AA; 93451 MW; 4144AD8C1FB7AE6D CRC64;
MSSLRVIFAF SVRCFVFSLV VQLRMRTLCT AAAADGNKTD HLSLLDFKAK IRHDPQYSLK
SWNDSVHFCN WDGVICSSKH RRVTVLDLQS KGLVGSLSPH VGNLSFLRQL ILQNNTLQGE
IPQEIGHLFR LQVLRLENNS FEGEIPSNLS HCSNLFFLRL GYNKLVGKIP VELSTLSNLI
RLSIIGNYFS GGIPPSLGNL SSLEVFAADG NLLDGTIPES FGKLKYLAYI GLHGNKLSGT
FPASIYNLSS IIFLLVSDNL LHGSIPSNIG LQLPHLQELE MWGNHFSGSI PVSLSNASEL
VYVDLGTNNF TGKVLSAHFG GLRHLSHLAL YQNSLGSNKD DDLDFITSLL NSTSFVFLDL
STNQLEGAFP NSVANLSSPL QWLSLGQNRI HGRLPSWLSG LVSLSRLSIQ FNQITGSIPS
DMGKLQNLYS MFFDHNRLTG IIPSSIGNLS FLNLLHLNDN NLHGTIPSSL GNCHELVFID
LSQNNLNGSI SDQLFALPTF FYCWFQHPKT EVVSDTLVLK SLEEVSYKSI LKATNGFSAE
SLIGAGSFGS VYKVILDEDG PALAIKVLNL QHRGASKSFM AECEALKSIR HRNLVKIITS
CTSIDFQGND FKALVYEYMP NGNLENWLHL GSGIGVAPFE TNSLSLLQRI DIAIDIGNAL
DYLHHQCERP IIHCDLKPSN VLLDIDMVAH IGDFGLAKFL PQLANPAQSS SMGVRGTIGY
APPEYGLGSE VSTSGDVYSY GILLLEMMTG KKPTDDNFTG NHNLHSICRM ALPDEVSEIV
DPILLQGDET NNNQGSMEPK AADSKVKCLI SMIKVGIACS MESPQDRMDI SNALTNLHYI
KSNYIRTREG K
//