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Database: UniProt
Entry: D7MUJ9_ARALL
LinkDB: D7MUJ9_ARALL
Original site: D7MUJ9_ARALL 
ID   D7MUJ9_ARALL            Unreviewed;       842 AA.
AC   D7MUJ9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Kinase family protein {ECO:0000313|EMBL:EFH40987.1};
GN   ORFNames=ARALYDRAFT_919378 {ECO:0000313|EMBL:EFH40987.1};
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).
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DR   EMBL; GL348720; EFH40987.1; -; Genomic_DNA.
DR   RefSeq; XP_002864728.1; XM_002864682.1.
DR   AlphaFoldDB; D7MUJ9; -.
DR   STRING; 81972.D7MUJ9; -.
DR   EnsemblPlants; scaffold_802778.1; scaffold_802778.1; scaffold_802778.1.
DR   GeneID; 9302504; -.
DR   Gramene; scaffold_802778.1; scaffold_802778.1; scaffold_802778.1.
DR   KEGG; aly:9302504; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_42_1_1; -.
DR   OrthoDB; 1212540at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IEA:EnsemblPlants.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0097275; P:intracellular ammonium homeostasis; IEA:EnsemblPlants.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IEA:EnsemblPlants.
DR   GO; GO:0080147; P:root hair cell development; IEA:EnsemblPlants.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045272; ANXUR1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_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; PTHR27003:SF296; OS03G0759600 PROTEIN; 1.
DR   PANTHER; PTHR27003; OS07G0166700 PROTEIN; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFH40987.1};
KW   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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..842
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003104492"
FT   TRANSMEM        424..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          525..803
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   842 AA;  92656 MW;  9D8FDC353186F1FC CRC64;
     MGGEFRHFSS HVSLLLLLFL VVKSSSSFTP ADNYLIDCGS SGETKLSDGR NFKSDQQSVA
     FLQTDEDIKT SVDSIPISDS NSSTLPLYLT ARIFAGKSTY SFYISRPGRH WIRLHFYPLN
     HPLYNLTNSV FSVTTDATVL LHDFSAGDTS SIAFKEYLIY AAEKLSLYFK PHKGSTAFIN
     AVEIVSVPDE LVPDSASSVP QAPDFKGLSS FSLEILHRIN IGGDLISPKI DPLSRTWLSD
     KPYNLFPEGS RNVTVDPSTI TYPDGGATAL IAPNPVYATA EEMADAQTSQ PNFNLSWRMS
     VDFGHDYFIR LHFCDIVSKS LNDLVFNVFI NKLSAISALD LSSLTNALGA AYYADFVLNA
     STITNGSILV QVGPTPSLQS GKPNAILNGL EIMKLNNAAG SLDGLFGVDG KYKGPIGGMS
     SKKLAIAGIG FVMALTALLG VVMLLVRWQR RPKDWQKQNS FSSWLLPLHA SHSSYISSKG
     GSTSRRMSIF GSKKSKSNGF SSFFSNQGLG RYFPFTELQI ATQNFDENSV IGVGGFGKVY
     IGEIDGGTQV AIKRGSQSSE QGINEFQTEI QMLSKLRHRH LVSLIGFCDE NKEMILVYEY
     MSNGPLRDHL YGSKENDPNP IPTLSWKQRL EICIGSARGL HYLHTGAAQG IIHRDVKTTN
     ILLDENLVAK VSDFGLSKDA PMEQGHVSTA VKGSFGYLDP EYFRRQQLTD KSDVYSFGVV
     LFEVLCARPV INPQLPREQV NLAEYAMNLH RKGMLEKIID PKIVGTISKG SLRKFVEAAE
     KCLAEYGVDR PGMGDVLWNL EYALQLQEAS AQVDLSEDKT TMNIEMDYIP GEEMQTPSHS
     VL
//
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