ID D7MDV9_ARALL Unreviewed; 674 AA.
AC D7MDV9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFH43986.1};
GN ORFNames=ARALYDRAFT_657778 {ECO:0000313|EMBL:EFH43986.1};
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:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; GL348719; EFH43986.1; -; Genomic_DNA.
DR RefSeq; XP_002867727.1; XM_002867681.1.
DR AlphaFoldDB; D7MDV9; -.
DR STRING; 81972.D7MDV9; -.
DR EnsemblPlants; Al_scaffold_0007_1833; Al_scaffold_0007_1833; Al_scaffold_0007_1833.
DR GeneID; 9303799; -.
DR Gramene; Al_scaffold_0007_1833; Al_scaffold_0007_1833; Al_scaffold_0007_1833.
DR KEGG; aly:9303799; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR OrthoDB; 893665at2759; -.
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:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR27002:SF1028; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 11; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..674
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003103549"
FT TRANSMEM 290..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..130
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 136..249
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 354..633
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 260..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 674 AA; 74954 MW; FF18FC2ED14C0C85 CRC64;
MNQRRTLFSI LCFFLISFGV ASVSAQTCTT DKGTFRPNST YDVNRRLILS SLPSNVTDQD
GLYYNGSIGQ EPNRVYAVGM CIPGSTSDDC SDCIKKASDE FLNNCPNQTE AYSWPGEPTL
CYVRYSNTSF SGSADLDPRV LLFNTGVIRS NLTEFTAIWE GLMGRMIATA STAKSTPSSS
NNHYSAEVAA LTTFEDMYAL MQCTPDLSIR DCENCLQRSA GDYQSCCSQN RGGVVMRPSC
FLRWDLYTYS NAFDNITVAS PPPEPPVTVP QGPQPAGDQA NTTDNDSKGI SAGVVVAIIV
PTVIVILILL VLGFVLFRRR KSYQRTEIES ESDISTTDSL VYDFKTIEAA TNKFSTSNKL
GEGGFGAVYM GKLSNGTEVA VKRLSKKSGQ GTREFRNEAV LVSKLQHRNL VRLLGFCLER
EEQILIYEFV HNKSLDYFLF DPEKQSQLDW TRRYKIIGGI ARGILYLHQD SRLKIIHRDL
KASNILLDAD MNPKIADFGL ATIFGMDQTQ GNTNRIAGTY AYMSPEYAMH GQYSMKSDIY
SFGVLVLEII SGKKNSGVYQ MDETSTAGNL VTYASRLWMN KSPLELVDPT FGRNYQSNEV
TRCIHIALLC VQENPEDRPM LSTIILMLTS NTITLPVPRL PGFFPRSRQL ELVSEGPESD
QSTSKSFPLL VRKK
//
