ID A0A118K6B8_CYNCS Unreviewed; 1067 AA.
AC A0A118K6B8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Leucine-rich repeat-containing protein {ECO:0000313|EMBL:KVI10443.1};
GN ORFNames=Ccrd_011223 {ECO:0000313|EMBL:KVI10443.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI10443.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI10443.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI10443.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVI10443.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LEKV01001020; KVI10443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118K6B8; -.
DR STRING; 59895.A0A118K6B8; -.
DR EnsemblPlants; KVI10443; KVI10443; Ccrd_011223.
DR Gramene; KVI10443; KVI10443; Ccrd_011223.
DR OMA; WRSADAN; -.
DR Proteomes; UP000243975; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1067
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007160002"
FT DOMAIN 759..1051
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1047..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1067 AA; 116480 MW; F5A170312BCA54EA CRC64;
MPHPHSTFSF ALLSIFIFFP YLSNSIDSQG HLLLSWKTTF KTAINDLQSW NPSDPTPCKW
FGIHCNSAAH VVAIRLNSID LQAPLPSNLH SLKFLESLVL SSTNLTGPIP AEFGDYLHLT
ELDISDNSIS GRIPPEICRL SNLHTLSLHT NSLEGEIPVE IGRLSSLRSL MIYDNRLSGR
IPKSIGQLGN LEVIRAGGNK NLDGELPEEI GNCSNLVMLG VAETSISGGI PASIGKLKRI
QTIAIYTSRL SGTIPDEIGN CSELRNLYLH QNSISGSIPK RIGELRKLES VLLWQNSLVG
TIPEELGSCN ELKTIDLSEN SLTGRIPASF GGLLKLRELQ LSVNQLSGTI PLEITNCTAI
THLELDNNQL TGEIPILIGR LRSMTLFFAW RNNLTGSIPE SLSQCHHLQA LDLSNNHLSG
TIGKEIFSLK NLRKLLLLSN DLSGSILPDI GNCTNLYRLR VNGNRFSGSI PSEIGNLKNL
NFLDMSSNRF VGVIPESISS CANLQFLDLH SNGLDGVIPN TLPISLQFVD ISDNRLEGPL
TPSIGLLTKL TKLNLGTNRL SGEVPWEIVS CGKLQLLDLG NNCYSGLLPK QLGQIPSLGI
SLNLSCNQFN GEIPAEFIGL AKLTSLDLSH NKLNGTLDVL KDLQNLVSLN VSFNDFTGQM
PNTPFFRNLP PAGTAGNPAL YFVSGVDTPP DEKGFAGHAR PAAKLAMSIL VSIGAILVLL
GTYMLVRTHL ANIKVDDETW EMTFYQKIEV SVDDIVRNLT TSNIIGTGSS GVVYRVTTMK
GETLAVKKMW STEQSGAFSS EIQTLGSIRH KNIIRLLGWG SNQTIKLLFY DYYPNGSLSS
LLHGAGKGAE WEDRYNILLG VAHALSYLHH DCMPAILHGD VKAMNVLLGS SLHPYLADFG
LARLVTNDQN GLSKQIQRPQ LAGSYGYMAP GSEQLPFFSL SKHASGQWIT EKSDIYSFGV
LLLEALTGKH PLDPTLPGSE HLVQWVREHL HGKQDPVDIL DPKLRGRADP QMHEMLQTLA
VSFLCVSPHP DDRPIMKDVV AMLKEIHHED STRSDPELKG GSSPAPG
//
