ID R0F9U0_9BRAS Unreviewed; 870 AA.
AC R0F9U0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN ORFNames=CARUB_v10007358mg {ECO:0000313|EMBL:EOA18762.1};
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:EOA18762.1, 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 -!- 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|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR000641};
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|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; KB870811; EOA18762.1; -; Genomic_DNA.
DR RefSeq; XP_006285864.1; XM_006285802.1.
DR AlphaFoldDB; R0F9U0; -.
DR STRING; 81985.R0F9U0; -.
DR GeneID; 17877754; -.
DR KEGG; crb:17877754; -.
DR eggNOG; ENOG502QU6U; Eukaryota.
DR OrthoDB; 364069at2759; -.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF52; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 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|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..870
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004349680"
FT TRANSMEM 440..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..156
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 513..805
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 844..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 870 AA; 95956 MW; DBD3C8B4AA42AEDF CRC64;
MTSTFLLSLF LSLINLLFVS VSCAPCTEFV YSNFTASNLR FIDSSKGAFL FSSNSIFKAG
LFRPGDDESS SNYYFSVVHV DSGSTIWSSN RDSPVSSSGK MNLTPQGISV VEDGKSQIPV
WSTPVLASPV YSLRLTDSGN LLLLDRLNVS LWESFDLPTD SIVLGQRLKV GKFLSGSVSR
SDFSTGDYKF LVDVSDGLMQ WRGQNYWKLK MHTRANVDSN FPVEYLTLTT SGLALMGRNG
TVVVRVALPP SSDFRVAKMD SSGKFTVSRF SGKSLVTEFS GPMDTCQIPY VCGKLGLCNL
DNASENQRCS CPEEMRSDAD KKVCVPVSQS MSLPVSCEAS NISYLQLGLG VSYFSTHFTD
PVDHGLALSA CHDLCSMNCS CLGVFYENTS RSCYLVKDSF GSLSLVKNSP DNQDLIGYVK
LSIKKPNGQP PGDKSRGSKF PVIALVLLPC SGFFLLIALG FIWWRRCAVM RYSSIREKQV
TRPGSFGSGD LGSFHIPGLP QKFEFEELEQ ATENFKDQIG SGGFGSVYKG TLPDETLVAV
KKITNHGLHG RQEFCTEIAI IGNIRHTNLV KLRGFCARGR QLLLVYEYMN HGSLEKTLFS
GNGPVLEWQE RFDIALGTAR GLAYLHSGCD QKIIHCDVKP ENILLHDHFQ PKLSDFGLSK
LLSQEESSLF TTMRGTRGYL APEWITNTAI SEKADVYSYG MVLLELVSGR KNCSFRSRSN
SVTEENNVNS SSTTTTSTGM VYFPLYALDM HEQGRYMELA DPRLEGRVTS QEVEKLVRIA
LCCVHEEPAL RPTMAAVVGM FEGSIPLGIP RMESLNFLRF YGLRFAESSM VEGQNGESET
MVFHRRESSN SAGSRHSASY IASQEVSGPR
//