ID A0A2J6LE29_LACSA Unreviewed; 1008 AA.
AC A0A2J6LE29;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=LSAT_2X55441 {ECO:0000313|EMBL:PLY85589.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY85589.1};
RN [1] {ECO:0000313|EMBL:PLY85589.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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:PLY85589.1}.
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DR EMBL; NBSK01004241; PLY85589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LE29; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_2X55441_mrna; cds-PLY85589.1; gene-LSAT_2X55441.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_2X55441_mrna; cds-PLY85589.1; gene-LSAT_2X55441.
DR OrthoDB; 306143at2759; -.
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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF561; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1008
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014466054"
FT TRANSMEM 633..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 694..984
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1008 AA; 110276 MW; BAE4320298BA7D53 CRC64;
MCFSFFSKVA VLFVALIIQM SGVVSVDNLA LHAIKSEITE DPQGVLKFWN DSLPFCLWRG
VICGSRHQRV TGLNLANRGL VGTLSPSIGN LSFLRYIYLD NNKLHGSIPS EIGSLFRLES
LSLPNNSFAK EIPNNISNCT KLQHIDLSGN MLSGNIPNIF SSLGMIQEIN FWKNKLTGGI
PTSIGNLTYL EFINLSGCRL EGSIPDSFHQ LTNLRSLILG ENRLVGNFPM FIFNLSKIEV
LNFPDNQLAG SLPSNLCSNQ PHLQRLEFGQ TLFTGVLPPS LSNCSQLRRF DSTYNNFKGE
INVDFGKLRH LWWLTLGPTE GLGGMKYFDS LLNCSNLELL ELAGLQLRGI PDWVGNLTEL
RTLKFQYTSI SGTLPSSIGN LHRLTVLSLV GNKLTGMIPE SIGKLSNLAY LNLGFNSFSG
IIPRSIGNLS SLIEISFREN KLEGTIPSSI GACKELIFLS FALNNLIGTI PKEVFQLSSL
SKALDLSVNN LSGVLPPGIH RLKNLDLFDL SMNHLSGEIP SSLSSCISLG LLDFSSNSFH
GSMPEAWRSL KGLKYLNLSR NNISGPIPSY LEQIPLEYLD LSYNDFEGEV YVKGVFTNTS
VVSVQGNPRL CGGIAELHLA KCTSIVSNKS KKLSLGGILA ISLSSVAACV ALVFFVLVYF
CVKKKKDTPT ESILIRESFE MFSYERLFKA TDGFSSQNLI GTGSFASVYK GVLDEEGTIV
AIKVLNLQRR GGSKSFIAEC EALRNIRHRN LVKIITACST LNFQGNDFKA LVYDFMPNGS
LERLLHSCTI LDHMPPHHSC QLDLIQRISI AKDVACALDY LHNHCGNVVV HCDLKPSNIL
LDVDMVAHIG DFGLAKILTL DQLPNANMSS SSLISGTIGY AAPEYGLGNG VSPEGDIYSY
GILLLEMVTG KRPIDLMFQE GLSLHSYARK ALADGFLLQI VDPMLLNDDV NEVFLSSLAK
IGVQCSYESP HDRMDIGIVI HELLSVMGTA SSMSTDKVGV SATQEASV
//
