ID D7MQ65_ARALL Unreviewed; 951 AA.
AC D7MQ65;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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_684582 {ECO:0000313|EMBL:EFH42053.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; GL348720; EFH42053.1; -; Genomic_DNA.
DR RefSeq; XP_002865794.1; XM_002865748.1.
DR AlphaFoldDB; D7MQ65; -.
DR STRING; 81972.D7MQ65; -.
DR EnsemblPlants; Al_scaffold_0008_1402; Al_scaffold_0008_1402; Al_scaffold_0008_1402.
DR Gramene; Al_scaffold_0008_1402; Al_scaffold_0008_1402; Al_scaffold_0008_1402.
DR eggNOG; ENOG502QQ5C; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR021720; Malectin_dom.
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; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF68; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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 4: Predicted;
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..951
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003104301"
FT TRANSMEM 558..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 618..901
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 920..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 951 AA; 105638 MW; 89FD3819D3C56CB6 CRC64;
MVTSHSMYFV IITTLLFSGI FESCNTTKLH DAEVRALKEI GKKMKKKDWD FSKDPCSGKG
NWIVNTNPLI NSNLTCDCSF HPPNSSCHVI AMILTRNCLT GSIPKEWASM RLEKLNLEGN
RFSGPIPPEI GKLVHLEELF LSSNSFTAHL PEQLGQLKNL TNMWISDNEF TGQIPNFIGN
LTKMVELEMF GSGLDGPLPS STSALTSLVN LQISDLGGKS SSFPPLQNMK SLKILELRRC
NIYGRLPKYI GDMTSLKTLD LSFNHLTDKI PSSLANLKLA DYIYLAGNKF TGGVPNSFIE
SNKNIDISSN NFTLQSSIPR GDCDQVNNAY KGYPCYFQHL PCLLPKRKYK YKLYINCGGD
EIKVDKEKTY EANIEGQRPT TFVYGSDKHW AFSSTGHFMN DLTEVDDYTV SNTSTLLANA
SSPSFVLYKT ARISPLLLTY YGLCLGNGEY TVSLHFAEII FTSDSTFYSL GKRVFDIYVQ
EKLMIKNFNI KEAAGGSGKP IIKTFVVNVT NHNLKISLRW AGKGTTTLPI RGVYGPMISA
ISVEPNFKSP EHDDKKNILL IVGIIVAAVI LILAIITVII CLWRRRCYKN AMDKELRGLD
LQTGTFTLRH IKAATNNFDA ANKIGEGGFG SVYKGVLSEG RMIAVKKLSS KSNQGSREFV
NELGMISSLQ HPNLVKLYGS CVEKKQLILV YEYLENNCLS RALFGSRLKL EWPTRKKICL
GIAKGLKFLH EESAIKIVHR DIKASNVLLD DDLNAKISDF GLAKLNDDEN THINTRIAGT
PGYMAPEYAM RGYLTEKADV YSFGVVALEI VSGKSNSNVK PSENLECLLD QAYVLQDKGC
LLDLVDPVLD SAYSKEEAMV ILNVALLCTN TSPALRPKMS QVVSLLEEKA AMKNLLSDPN
FSAVNPKLKA LRKFFWQSEA STSGPRTTDN VDADENSSKD EIVEVPELEC E
//
