ID B9S8F9_RICCO Unreviewed; 965 AA.
AC B9S8F9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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_1252420 {ECO:0000313|EMBL:EEF40136.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; EQ973891; EEF40136.1; -; Genomic_DNA.
DR AlphaFoldDB; B9S8F9; -.
DR eggNOG; ENOG502QTAM; Eukaryota.
DR InParanoid; B9S8F9; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF105; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF40136.1};
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:EEF40136.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..965
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005666406"
FT TRANSMEM 592..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 649..965
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 896..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 965 AA; 108535 MW; 3E599755B84B4577 CRC64;
MLSRCMHLLL VVLSGFGCIL CRMQLHRDEE LTLIQIQSTL GAQGFQLSLD CPSSVTVLKK
KGQPEDEMEE SGVRCDCPND FSNSCHITDF VLKSFSLPGS LPPELANLKY LEKIDLTRNY
LQGKIPEEWA SLQNLKYLSL TANRLSGNIP KYLERFTSLT YLSLEANQFS GTIPPELGNL
VSLNDLMLSS NQLEGNLPEK LAQLKNLTNF RVSDNNLSGT IPTFIQNWNQ LGRLELQASG
LEGPVPAGIF HLQNLTDLRI SDVSGPEFQF PNVSKKLKYL VLRNINLFGK IPEITWKLEK
LRLLDVTFNK LQGGIPFDAK LPNYTFLTHN MLTGNVPDNI SQNKTVDLSY NNLSWPSNCQ
EKININTYRS SSFKKNFGLL PCFNLSVCKK YYSSFHINCG GPDKVVKNGY GKLSYEGDQG
IQGGAARNYI KETNWGFSST GDYMDDSDYY NNKYTLSSDS NLSEIYLTAR KAPLSLTYYG
YCLENGNYTV KLHFAEIQFT DEKAYNRAAR RIFDIYVQGK LIWKDFNIVK EANGSNRYIT
RVCNASVVDN TVEIRLYWAG KGTTIIPRRG NYGPIISAIS VCFEPEESKR PIIIAVATSV
SLLVFLVICA LCWKFCFQKK YKRDKDLRGV DLQTGSFTLR QLRAATNNFD CTRKIGEGGF
GSVYKGELSD GTVIAVKQLS SKSRQGNREF VNEIGMISGL QHPNLVKLYG CCTEGNQLLL
VYEYMENNSL ARALFETRVL KLDWATRQKI CVGIARGLAF LHEESTLRIV HRDIKGTNVL
LDKDLNAKIS DFGLAKLSEE ENTHISTRIA GTVPKDEGIC LLEWAFILRQ KGHLTDIVDP
RLESEFNKEE AERMIRMALL CTNESPTLRP TMSAVVSMLE GETSVEEVIS DPSIYVDDMR
YKPPKDHYQQ TQRKSSSGSQ RLNFSSDNTG VGSSSVSTTS AHHDLYPLNH QSIELNFSEI
SSLSQ
//
