ID R0FB96_9BRAS Unreviewed; 660 AA.
AC R0FB96;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CARUB_v10003320mg {ECO:0000313|EMBL:EOA19322.1};
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:EOA19322.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family.
CC {ECO:0000256|ARBA:ARBA00010217}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000256|ARBA:ARBA00008536}.
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DR EMBL; KB870810; EOA19322.1; -; Genomic_DNA.
DR RefSeq; XP_006286424.1; XM_006286362.1.
DR AlphaFoldDB; R0FB96; -.
DR STRING; 81985.R0FB96; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR Proteomes; UP000029121; 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27007; -; 1.
DR PANTHER; PTHR27007:SF192; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE VI.2; 1.
DR Pfam; PF00139; Lectin_legB; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..660
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004340403"
FT TRANSMEM 280..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 337..611
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 660 AA; 73081 MW; 0AA6DC45E67EEFFB CRC64;
MATQRSMVSV SCLFKLFLFL SVHVRAQRTI TTEFTFRGFS GNQSEIRMEG AAMIKPNGLL
RLTDRKSNVT GTAFYHKPVK LLETSRDSTN VTIGSFSASF VFVIIPSSST NKGFGFTFTL
SPTPYRANAG SAQYLIGNDI GLNYNSRTSD IQEPVVYYSN DDPNKKEDFQ LESGNPIQAL
VEYDGPTQML NVTVYPARLG FKPTKPLISR HVPKLLEIVQ QEMYVGFTAS TGRGQSSAHY
VMGWSFSSGG DRPKADVLNL SELPPPPPNT AKKSGVNSQV IVLVVALSAV MLVMLVLLFF
FFMYKKRLGQ EETLEDWEID HPRRLKYRDL YEATDGFKET RIIGTGGFGT VFKGKLPSSD
LIAVKKIIPS SMQGVREFVA EIESLGKLRH KNLVNLQGWC KHKNDLLLIY DYIPNGSLDS
LLYTVPRRSG AVLSWNVRFE ISKGIASGLL YLHEEWEKIV IHRDVKPSNV LIDSKMNPRL
GDFGLARLYE RGALSQTTAL VGTIGYLAPE LARNGKPSTA SDIFAFGVLL LEIVSGRRPT
GSGSFFLVDW VMELHANGEI LSAMDPRLGS GYDGGEARIA LAVGLLCCHQ NPESRPSMRN
VLRYLNGDEN VPEIEDDRGY SNPSRNEFGS RFEGYDSSSS GAFSFVNRVS STFRISDGNG
//
