ID D7KGV3_ARALL Unreviewed; 507 AA.
AC D7KGV3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein kinase BSK {ECO:0000256|RuleBase:RU369005};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU369005};
DE AltName: Full=Brassinosteroid-signaling kinase {ECO:0000256|RuleBase:RU369005};
GN ORFNames=ARALYDRAFT_892050 {ECO:0000313|EMBL:EFH67864.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Serine/threonine kinase that acts as positive regulator of
CC brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
CC {ECO:0000256|RuleBase:RU369005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|RuleBase:RU369005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|RuleBase:RU369005};
CC -!- SUBUNIT: Interacts with BRI1. {ECO:0000256|RuleBase:RU369005}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193,
CC ECO:0000256|RuleBase:RU369005}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004193, ECO:0000256|RuleBase:RU369005}.
CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684,
CC ECO:0000256|RuleBase:RU369005}.
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DR EMBL; GL348713; EFH67864.1; -; Genomic_DNA.
DR RefSeq; XP_002891605.1; XM_002891559.1.
DR AlphaFoldDB; D7KGV3; -.
DR STRING; 81972.D7KGV3; -.
DR EnsemblPlants; scaffold_104844.1; scaffold_104844.1; scaffold_104844.1.
DR GeneID; 9327667; -.
DR Gramene; scaffold_104844.1; scaffold_104844.1; scaffold_104844.1.
DR KEGG; aly:9327667; -.
DR eggNOG; ENOG502QQT6; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR OrthoDB; 651092at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045845; BSK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45863; SERINE/THREONINE-PROTEIN KINASE BSK5; 1.
DR PANTHER; PTHR45863:SF14; SERINE_THREONINE-PROTEIN KINASE BSK11; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369005};
KW Brassinosteroid signaling pathway {ECO:0000256|RuleBase:RU369005};
KW Cell membrane {ECO:0000256|RuleBase:RU369005};
KW Kinase {ECO:0000256|RuleBase:RU369005};
KW Lipoprotein {ECO:0000256|RuleBase:RU369005};
KW Membrane {ECO:0000256|RuleBase:RU369005};
KW Myristate {ECO:0000256|ARBA:ARBA00022707, ECO:0000256|RuleBase:RU369005};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369005};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU369005};
KW Transferase {ECO:0000256|RuleBase:RU369005}.
FT DOMAIN 75..332
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 11..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57683 MW; D56EB2BAB8B7906C CRC64;
MGCCQSSFLK PSSLHDKKIP SDDISGRRGK GAKRGNRHRH PNVNEGRGWL FSAVPDFSEF
SASVLRDATN NFNKNAVVSV CSDQEPNVVY QGCIKSDKDK RLIAVKKFSK TTWPDPKQFA
AEARAIGNLR HVRLVNLIGY CCDGDERLLV SEYMPNQSLT KHLFHWEKQT MEWAMRLRVA
LYVAEALEYC RQSGLKLYHD LNTCRVLFDE NGSPRLSCFG WMKNSKDGKN FSTNLAYTPP
EYLRSGTLIP ESVVFSFGTF LLDLLSGKHI PPSHAVDTIQ KQNLIVLMDS HLEGNYPEED
AAMVFDLASK CLHNNPNERP EIRDIISVIA TLQQKLDVPS YTMLGISKLE KLEMERPKSL
IYDACHQKDL EALHQILEAM EYKEDEVTCE LSFQQWAQQI KDVCNTRQQG DSAFRNKNFE
SAIEKYTQFI ETGIMISPTV YARRSMCYLF CDQPDAALRD AMQAQCVYSD WPTAFYLQAV
ALSKLNMVED SANMLKEALI LEDKRGS
//
