ID A0A078FF38_BRANA Unreviewed; 735 AA.
AC A0A078FF38;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=BnaC06g31470D {ECO:0000313|EMBL:CDY11592.1};
GN ORFNames=GSBRNA2T00049706001 {ECO:0000313|EMBL:CDY11592.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY11592.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY11592.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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DR EMBL; LK032012; CDY11592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078FF38; -.
DR STRING; 3708.A0A078FF38; -.
DR PaxDb; 3708-A0A078FF38; -.
DR EnsemblPlants; CDY11592; CDY11592; GSBRNA2T00049706001.
DR Gramene; CDY11592; CDY11592; GSBRNA2T00049706001.
DR OMA; MMPRVLM; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR047117; PERK1-13-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR47982; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK4; 1.
DR PANTHER; PTHR47982:SF19; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 385..661
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 735 AA; 78037 MW; C14B0769E79CC112 CRC64;
MSDSPSSSPP APSADSGSPP DNSTGASAPP PADSAPPPTP PPDNSTGGSA PPPANSAPPP
SPPADSTPPP DSSSPPPATP PPVSEPPPPP PDSPPPPPPD APPPADPTPV DSGSPPPKPT
TSPPPPPEES ESPPPPPNEE DSSPPPPPPE KSSPPPSEKS SPPPPEKSSS PPSEKSSPPP
ASSPKAAPKK KKKSPPPPPG VPTKSPSAPT KSPPNAPPPL KAPHALPPKS AAAGGPLKSP
STGVSSFPPP PPNSNDNGYQ GKTMAGMAVA GFAIIAVVAV LFFVRRKKKR NVDAYSDSQY
LPPPNFSIQS DGLLHGQNTT KGYSVPGGYN TQQQSYNTQQ QSDNTRTSFG SQRGSQRGYP
PDSAVMGSGQ THFTYEELMD ITEGFAQRNI LGEGGFGCVY KGKLHDGKLV AVKQLKVGSG
QGDREFKAEV EIISRVHHRH LVSLVGYCIS DVERLLIYEY VPNQTLEHHL HGKGRPVLEW
AKRVRIAIGS AKGLAYLHED CHPKIIHRDI KQSSFFSKPF AVADFGLAKL NDSTQTHVST
RVMGTFGYLA PEYAQSGKLT DRSDVFSFGV VLLELVTGRK PVDQYQPLGE ESLVEWARPL
LHKAIETGDF SDLVDRRLQN HYVENEVFRM IETASACIRH SGPKRPRMAQ VVRALDSEGD
MGDISNGSKV GQTSSNDSGQ YNSDAMKFRK MAFGFDDSSD SGDYSVRSSS RGSYGASTEF
TRNESENRNF NNRQF
//
