ID R0I8X3_9BRAS Unreviewed; 661 AA.
AC R0I8X3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CARUB_v10022069mg {ECO:0000313|EMBL:EOA34525.1};
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:EOA34525.1, 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; KB870806; EOA34525.1; -; Genomic_DNA.
DR RefSeq; XP_006301627.1; XM_006301565.1.
DR AlphaFoldDB; R0I8X3; -.
DR STRING; 81985.R0I8X3; -.
DR GeneID; 17895337; -.
DR KEGG; crb:17895337; -.
DR eggNOG; ENOG502QTAM; Eukaryota.
DR OrthoDB; 22648at2759; -.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0098542; P:defense response to other organism; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.200; -; 1.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27007; -; 1.
DR PANTHER; PTHR27007:SF241; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE V.2-RELATED; 1.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..661
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004342937"
FT TRANSMEM 282..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..620
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 661 AA; 72950 MW; C81D5D27009952D4 CRC64;
MSLLLKMLLL FSFFCFFTVD SVSQGSDPTG GQFSFNGFLY TDGVADLNPD GLFKLITSKT
QGGAGQVLYQ FPLQFKNSPN GKVSSFSTTF VFAIVAVRKT VSGCGLSFNI SPTKGLSSVP
NINHSSSSNR SVSVELHTAK SDKPDGEDIK LVGVKVDSLQ TDGNCSAGYY KDDGRLVNLD
IASGKPIQVW IEYNNSTKQL DVTMHSIKIS KPKIPLISLR KDLSPYLLEY MYTGFTSVGS
PTSSHYILGW NFNNSGAVSD INLSRLPKVP DEDEDRRLSS KILAISLSIS GVTLVIVLVL
GIMFFLKRKK FLEVLDDWEV QFGPHKFTYK DLFVATKGFK NSELLGKGGF GKVFKGILPL
SSIPIAVKKI SHDSRQGMRE FLAEIATIGR LRHPDLVRLL GYCRRKGELY LVYDYMPKGS
LDKFLYNQPN QILDWSQRFK IIKDVASGLC YLHQQWVQVI IHRDIKPANI LLDENMNAKL
GDFGLAKLCD HEIDSQTSNV AGTFGYISPE LSRTGKSSTS SDVFAFGVFM LEITCGRRPI
EPRGSPSEMV LSDWVLDSWD SADILHVVDE RLGHRYLAEQ ITLVLKLGLL CSHPVAATRP
SMSSVIQFLD GVATLPHNLL DLVNAHIIDG GFYALGESIE SRGDSSNVSV VMTESFLSSG
R
//
