ID A0A078GWD1_BRANA Unreviewed; 593 AA.
AC A0A078GWD1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=BnaA06g15010D protein {ECO:0000313|EMBL:CDY29469.1};
GN Name=BnaA06g15010D {ECO:0000313|EMBL:CDY29469.1};
GN ORFNames=GSBRNA2T00043133001 {ECO:0000313|EMBL:CDY29469.1};
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:CDY29469.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY29469.1, 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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; LK032238; CDY29469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078GWD1; -.
DR STRING; 3708.A0A078GWD1; -.
DR PaxDb; 3708-A0A078GWD1; -.
DR EnsemblPlants; CDY29469; CDY29469; GSBRNA2T00043133001.
DR Gramene; CDY29469; CDY29469; GSBRNA2T00043133001.
DR OMA; IVERNHY; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF322; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..593
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001736231"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..179
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 180..222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 267..539
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DISULFID 145..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 593 AA; 65662 MW; 8C02C53885A61575 CRC64;
MNKVHGLFLV AIFSIVYTQL VNGHSLRGCQ NKCGNLSIEY PFGTSPGCYY VEDPSFLLTC
NETTNELFYG VNMQVINISH SGELRFLKSP SFSCYNSTDL TDRITYNTTL GNFTLSNKNK
FTAVGLLDWS IGGQTCQQVA NKSICGTNSL CLDSTTGTGY NCKCKAGYDG NPYLPEGCQD
IDECTTSSTI HKHNCSDSST CVNTMGHFLC SCPSGFDLNA TTNGCMRKHK PENHPWIIIV
LGTTVGLFAI LLVTICVQQK MRHMKNIELR KQFFEQNGGG MLRQRLSGAG PSNVDVKIFT
EEGMKKATNG YDETRILGQG GQGTLLGCCL ETEVPLLVYE FINSGTLYDR LHGSMSDSSL
TWEHRLRIAV EIAGTLAYLH SSASIPIIHR DVKTANILLD ENVTAKVADF GASRLIPMDK
EQLTTMVQGT LGYLDPEYYN TGLLNEKSDV YSFGVVLMEL LSGQKALCFE KPQQSKHLVN
YFASAMKENR LHEVIEGQVM KENNQREIHE ASRIAVECTR LMGEERPRMK EVAAQLEALR
VGKTKHEGSD QYNEPEVNEH LVGVEMLSAQ GDTSTTGYDS MKNVTRLHIE AGR
//
