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Database: UniProt
Entry: A0A103YKY7_CYNCS
LinkDB: A0A103YKY7_CYNCS
Original site: A0A103YKY7_CYNCS 
ID   A0A103YKY7_CYNCS        Unreviewed;       607 AA.
AC   A0A103YKY7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Leucine-rich repeat-containing protein {ECO:0000313|EMBL:KVI10945.1};
GN   ORFNames=Ccrd_010652 {ECO:0000313|EMBL:KVI10945.1};
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:KVI10945.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVI10945.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVI10945.1};
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:KVI10945.1}.
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DR   EMBL; LEKV01000974; KVI10945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103YKY7; -.
DR   STRING; 59895.A0A103YKY7; -.
DR   EnsemblPlants; KVI10945; KVI10945; Ccrd_010652.
DR   Gramene; KVI10945; KVI10945; Ccrd_010652.
DR   OMA; FRQDFNN; -.
DR   Proteomes; UP000243975; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; 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; PTHR47988:SF11; BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR KINASE 1; 1.
DR   PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 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   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007119827"
FT   TRANSMEM        230..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          293..570
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          204..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   607 AA;  67280 MW;  0EFA5EC6562C49CB CRC64;
     MDRPVSLISA SALVWFILVF NILSNVYGNA EGDALNALKT QLGDPNNVLQ SWDATLVNPC
     TWFHVTCNND NSVTRVDLGN ANLSGQLVPQ LGQLTNLQYL ELYSNNITGR IPNELGNLTN
     LVSLDLYLNR LDGTIPDTLG KLQRLRFLRL NNNTLTGTIP VSLTTITSLQ VLDLSNNLLR
     GDVPVNGSFS LFTPISFANN PELRAPAVTP QTPSPPSSQS PSVANSATGA IAGGVAAGAA
     LLFAGPAIAL AWWRRRKPQD HFFDVPAEED PEVHLGQLKR FSLRELQVAT DNFSNRNILG
     RGGFGKVYKG RLADGSLVAV KRLKEERTQG GEMQFQTEVE MISMAVHRNL LRKREVRGVI
     SNELIIVITV ERPDAQDPLD WPIRKRIALG SARGLAYLHD HCDPKIIHRD VKAANILLDE
     EFEAVVGDFG LAKLMDYKDT HVTTAVRGTI GHIAPEYLST GKSSEKTDVF GYGVMLLELI
     TGQRAFDLAR LANDDDVMLL DWVKGLLKEK KLETLVDGDL RGNYIDEEVE QLIQVALLCT
     QGTPLERPKM SEVVRMLEGD GLAERWEEWQ KEEMFRQDFN STHNPNTDWI IADSTYNLRP
     DELSGPR
//
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