ID A0A078G8E1_BRANA Unreviewed; 729 AA.
AC A0A078G8E1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=BnaA09g44200D protein {ECO:0000313|EMBL:CDY21669.1};
GN Name=BnaA09g44200D {ECO:0000313|EMBL:CDY21669.1};
GN ORFNames=GSBRNA2T00016155001 {ECO:0000313|EMBL:CDY21669.1};
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:CDY21669.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY21669.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000671};
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DR EMBL; LK032123; CDY21669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078G8E1; -.
DR STRING; 3708.A0A078G8E1; -.
DR PaxDb; 3708-A0A078G8E1; -.
DR EnsemblPlants; CDY21669; CDY21669; GSBRNA2T00016155001.
DR Gramene; CDY21669; CDY21669; GSBRNA2T00016155001.
DR OMA; TIRMSHI; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013695; WAK.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF550; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08488; WAK; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Signal {ECO:0000256|SAM:SignalP}; 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..729
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001735673"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 421..667
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 668..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 80580 MW; BA1930B035CB8F63 CRC64;
MRSNTNYSLS TLLSPLLMLM LASKVVTLSG LCQSESCGGI KIQYPFGIQE RCYLNEWYKV
ECRNSTIPFL SKMGREVVNI SFEGDEDGGY YSYRQSFGSV RVKSQITSFG CSRNGQESKP
VLNLTNSPFF FGRGNSLVAV GCNSKASLTN IEPAKLECEL NCTATLPTKS VPFLDNTGCS
SNALSYAYRP QVCANNQGEE ERSCNGNGCC RASLPDDAEA QQVIGVRIES FDQGNSTTGG
CRVAFLTDEV YMSSNATEPQ SFFAKGYSTV TIRWVVKTTN LSFLNSLNCI DSEEYDSLPY
KTQQRRACIC NNITISGSNY ANCACNRGYT GNPYLLNGCQ DVNECLLSYG EGRYTCQKSH
TCVNEPGSVD CVEKKTVAIL IGVGSGIGIL VLVSGVWWLR KFLKKRRITQ KKRKCFKRNG
GLLLQQQLNT RESTVYKGML VDGRTVAVKK SKAVDEDKLE EFINEVVILS QVNHRHVVKL
LGCCLETEVP VLVYEFIPNA GALSYLHSAA SSPIYHRDVK STNILLDEKY RAKVSDFGTS
RTVTVDQTHW TTLVSGTVGY MDPEYYGSSQ YTDKSDVYSF GVVLVELITG EKPVLTLSNT
QEIKGLADHF RAAMKEDKFF DIMDARIRDA CKPEQVMAVA NLARRCLNSK GKKRPYMREV
FAELEKISSS QEVKTENDNG DDEEEEEGMD MIVMADSWTI GITGPASSTV ASSSSLDVEP
LLKTHGPVP
//
