ID R0G345_9BRAS Unreviewed; 1155 AA.
AC R0G345;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=CARUB_v10012845mg {ECO:0000313|EMBL:EOA29756.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29756.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KB870807; EOA29756.1; -; Genomic_DNA.
DR RefSeq; XP_006296858.1; XM_006296796.1.
DR AlphaFoldDB; R0G345; -.
DR STRING; 81985.R0G345; -.
DR GeneID; 17890881; -.
DR KEGG; crb:17890881; -.
DR eggNOG; ENOG502QSHG; Eukaryota.
DR OrthoDB; 449350at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
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; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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}; Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 816..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 878..1150
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 776..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 906
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1155 AA; 125768 MW; 18AF37B830FDB9B1 CRC64;
MTSLPSSVIK WRFFRRQMPS HVVFSLWLFC FATCLSGKIT VLADSDKSVL LRFKTTVSDP
GALLASWVED SEDYCSWFGV SCDSTSRVMA LNISGSGSDK GSSKISRNRF TCGDIGKFPL
YGFGIRRDCT GNHGALVGNL PSVVVGLTEL RVLSLPFNSF SGEIPVGIWG MEKLEVLDLE
GNLMTGSLPV QFTGLRNLRV LNLGFNRVSG EIPNSLQNLS KLEILNLGGN WLNGTVPAFV
GSFRVVHLPL NWLQGSLPKD IGDNCGKLEH LDLSGNFLTG RIPESLGKCG SLRSLLLYIN
TLEETIPLQF GNLQKLEVLD VSRNTLSGPL PVELGNCTSL SVLVLSNLYN VYDDINSIRG
GADLPPGADL TSMTEDFNFY QGGIPEEITR LPKLKILWVP RATLEGRFPG DWGFCQNLEM
VNLGQNFFKG EIPVGLSKCR NLRLLDLSSN MLTGELLKDI SVPCMSVFDV GGNSLTGLIP
EFSNNTTAHC PPVVYIDRFS IESYNDPSSV YLSFFTMKAQ VGTSLMDFGG DGGPSVFHNF
ADNNFTGTLK SVPLAQERLG KRISYIFSAG GNQLYGQFPG NLFDKCDQLK AVYVNVSFNK
LSGRIPEGIN NMCTSLKILD ASSNQIFGTI PSGLGDLGSL VALNLSCNQL QGQIPGSLGK
KMTALTYLSI ANNNLTGQIP QSFGQLHSLS VLDLSSNYLS GGIPHDFVNL RNLTVLLLNN
NNLSGPIPSG FATFAVFNVS FNNLSGPLPS TNGLTKCSTV SGNPYLRPCH VFSLTTPSSD
PRDSTGDSIT QDYASSPVEN SPSQSSGKGG FNSLEIASIA SASAIVSVLI ALVILFFYTR
KWHPKSKIMA TTKREVTMFM DIGVAITFDN VVRATGNFNA SNLIGNGGFG ATYKAEISQD
VVVAIKRLSI GRFQGIQQFH AEIKTLGRLR HPNLVTLIGY HASETEMFLV YNYLPGGNLE
KFIQERSTRD WRVLHKIALD IARALAYLHD QCVPRVLHRD VKPSNILLDD DCNAYLSDFG
LARLLGTSET HATTGVAGTF GYVAPEYAMT CRVSDKADVY SYGVVLLELL SDKKALDPSF
VSYGNGFNIV QWACMLLRQG RAKEFFTAGL WDAGPHDDLV EVLHLAVVCT VDSLSTRPTM
KQVVRRLKQL QPPSC
//
