ID D7MTL3_ARALL Unreviewed; 1036 AA.
AC D7MTL3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=ARALYDRAFT_495467 {ECO:0000313|EMBL:EFH40547.1};
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; GL348720; EFH40547.1; -; Genomic_DNA.
DR RefSeq; XP_002864288.1; XM_002864242.1.
DR AlphaFoldDB; D7MTL3; -.
DR STRING; 81972.D7MTL3; -.
DR EnsemblPlants; fgenesh2_kg.8__1283__AT5G53890.1; fgenesh2_kg.8__1283__AT5G53890.1; fgenesh2_kg.8__1283__AT5G53890.1.
DR Gramene; fgenesh2_kg.8__1283__AT5G53890.1; fgenesh2_kg.8__1283__AT5G53890.1; fgenesh2_kg.8__1283__AT5G53890.1.
DR eggNOG; ENOG502QT4D; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR OrthoDB; 377080at2759; -.
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:0001653; F:peptide receptor activity; IEA:EnsemblPlants.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
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; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF62; OS02G0116700 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 9.
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, 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|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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1036
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003104160"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 754..1025
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1036 AA; 114043 MW; A13591ABAEF73F2C CRC64;
MVIILLLAFF VGSSVSLTCH PNDLSALREF AGALKNMSVT EPWLNGSRCC EWDGVFCEGG
DVSGRVTKLV LSDKGLEGVI SGSLGELSEL RVLDLSRNQL KGDLPVEISK LEQLEVLDLS
HNLLSGSVLG AVSGLKLIQS LNISSNSLSG NLSDVGVFPG LVMFNVSNNL FEGEIHPELC
SSSGEIQVLD LSMNRLVGNL DGLYNCSKSI QRLHVNSNGL TGQLPDYLYL IRDLEQLSVS
GNYLSGQLSQ NLSNLSGLKS LLISENRFSG VIPDVFGNLT QLEHLDVSSN KFSGRFPPSL
SQCSKLRVLD LRNNSLSGSI NLNFTGFTDL CVLDLASNHF SGPLPDSLGH CPKMKILSLA
KNEFSGKIPD TFKNLDSLLF LSLSNNSFVD FSETMNVLQH CRNLSTLILS KNFIGEEIPS
NVTGFNNLAT LALGNCGLRG QIPSWLLNCK KLEVLDLSWN HIYGTIPHWI GKMESLFYID
FSNNTLTGEI PVAITELKNL IHLNCTASQM TTSSGIPLYV KRNKSSSGLP YNQVSRFPPS
IYLNNNRLNG TILPEIGRLK ELHMLDLSRN NFSGRIPDSI SGLDNLEVLD LSYNHLYGSI
PLSFQSLTFL SKFSVAYNRL TGAIPSGGQF YSFPHSSFEG NLGLCRAIDS PCDVLMSNML
NPKGPSRSNN TGGRFGRSSI VVLTISLAIG ITLLLSVILL RISRKDSDDR INDVDEETIS
GVPKALGPSK IVLFHSCGCK DLSVEELLKS TNNFSQANII GCGGFGLVYK ANFPDGSKAA
VKRLSGDCGQ MEREFQAEVE ALSRAEHKNL VSLQGYCKHG NDRLLIYSFM ENGSLDYWLH
ERVDGNMTLK WDVRLKIAQG AARGLAYLHK VCEPNVIHRD VKSSNILLDE KFEAHLADFG
LARLLRPYDT HVTTDLVGTL GYIPPEYSQS LIATCRGDVY SFGVVLLELV TGRRPVEVCK
GKSCRDLVSW VFQMKSEKRE AELIDTTIRE NVNEKTVLEM LEIACKCIDH EPRRRPLIEE
VVTWLEDLPM ESVQQQ
//
