ID D7LNA6_ARALL Unreviewed; 1013 AA.
AC D7LNA6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=ARALYDRAFT_347816 {ECO:0000313|EMBL:EFH53804.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; GL348717; EFH53804.1; -; Genomic_DNA.
DR RefSeq; XP_002877545.1; XM_002877499.1.
DR AlphaFoldDB; D7LNA6; -.
DR STRING; 81972.D7LNA6; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_5001208; fgenesh1_pg.C_scaffold_5001208; fgenesh1_pg.C_scaffold_5001208.
DR GeneID; 9313613; -.
DR Gramene; fgenesh1_pg.C_scaffold_5001208; fgenesh1_pg.C_scaffold_5001208; fgenesh1_pg.C_scaffold_5001208.
DR KEGG; aly:9313613; -.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR OrthoDB; 911668at2759; -.
DR Proteomes; UP000008694; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008:SF526; (RAPE) HYPOTHETICAL PROTEIN; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1013
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003102146"
FT TRANSMEM 647..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 705..1005
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1013 AA; 111558 MW; D87697EFA8D2DF9B CRC64;
MKSMMRLFLV LAFNALMLLE AYGFTGESDR QALLEFKSQV SEGKRNALSS WNNSFPLCSW
KGVRCGRKHK RVTRLDLGGL QLGGVISPSI GNLSFLIYLE LSNNSFGGII PQEMGNLFRL
KYLAIGFNYL GGRIPASLSN CSRLLYLDLF SNNLGEGVPS ELGSLTKLLY LYLGLNDVKG
KFPVFIRNLT SLIVLNLGYN NLEGEIPDDI ARLSQMVSLT LTMNKFSGVF PPAFYNLSSL
ENLYLLGNGF SGNLKPDFGN LLPNIRELSL HGNFLTGAIP TTLTNISTLE MFGIGKNRMT
GSISPNFGKL QNLHYLELAN NSLGSYSFGD LEFLDALTNC SHLHGLSVSY NRLGGALPTS
IVNMSAELTV LNLKGNLIYG SIPQDIENLI GLQSLLLADN LLTGPLPTSL GKLVGLGELI
LFSNRISGEI PSFIGNVTQL VKLNLSNNSF EGMVPPSLGD CSHMLDLQIG YNKLNGKIPK
EIMQIPTLVH LNMEGNSLSG SLPNDVGRLQ NLVELSLGNN NLSGQLPQTL GKCLSMEVMY
LQGNYFDGAI PDIKGLMGVK RVDLSNNNLS GGIPEYFENF SKLEYLNLSI NNFEGRVPTK
GKFQNSTTVF VFRNKNLCGG IKELKLKPCI VQTPPMGTKH PSLLRKVVIG VSVGIALLLL
LFVVSLRWFK KRKKNQKTNN SALSTLDIFH EKISYGDLRN ATDGFSSSNM VGLGSFGTVF
KALLPTESKT VAVKVLNLQR HGAMKSFMAE CESLKDIRHR NLVKLLTACA SVDFQGNEFR
ALIYEFMPNG NLDMWLHPEE VEEIRRPSRT LTLLERLNIA IDVASALDYL HVYCHEQIVH
CDIKPSNVLL DDDLTAHVSD FGLARLLLKF DQESFYNQLS SAGVRGTIGY AAPEYGMGGQ
PSIHGDVYSF GVLLLEMLTG KRPNNELFGG NFTLHSYTKS ALTEGVLDIA DVSILHSGLR
IGFPISECLT LVLEVGLRCC EESPTNRLAT TEVVKELITI RERFFKARRT ARR
//
