ID A0A078FD17_BRANA Unreviewed; 1267 AA.
AC A0A078FD17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=BnaC01g14390D protein {ECO:0000313|EMBL:CDY10824.1};
GN Name=BnaC01g14390D {ECO:0000313|EMBL:CDY10824.1};
GN ORFNames=GSBRNA2T00048684001 {ECO:0000313|EMBL:CDY10824.1};
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:CDY10824.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY10824.1, 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: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LK032007; CDY10824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078FD17; -.
DR PaxDb; 3708-A0A078FD17; -.
DR EnsemblPlants; CDY10824; CDY10824; GSBRNA2T00048684001.
DR Gramene; CDY10824; CDY10824; GSBRNA2T00048684001.
DR OMA; YEINEVT; -.
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-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 2.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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:SF951; BNAA01G12670D PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF01657; Stress-antifung; 4.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51473; GNK2; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
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:UP000028999};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1267
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001734449"
FT TRANSMEM 202..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..180
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 263..542
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 608..715
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 721..834
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 938..1217
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 966
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1267 AA; 140339 MW; 4E685FF03D3DC709 CRC64;
MKQWSLFSIL CFVLISFGIA SVSAQTCMDN DGHFRPNGTY DTNRRLILSS LPSNVTTQEG
LFFNGSIGQE PNRVYAIGMC IPGSTPQDCS DCLVVRMIDA ASTAKSTPSS SNNHYKADMA
LLTALENIYA LMQCTPDLSS GDCDNCLRQS ARDYQSCCGQ KQGGAFDNIT VASSPPPLPP
MASPSPGDDQ ARRTNNEDSK GISPGVVAAI TVPTVIILLV LGVVLCRRRM SMQRTDVESD
SDISTAQSSQ YDLKTIEAAT NKFLMSNKLG EGGFGEVYKG TLSNGTEVAV KRLSKKSGQG
IREFKNEAVL VSKLQHRNLV RLLGFCLEGD EKILIYEFVP NKSLNHFLFD PKKQSQLNWT
KRYKIIGGIA RGILYLHQDS QLTIIHRDLK ASNILLDANM NPKISDFGLS TIFGMEQTRG
NTSRIAGTYG YMSPEYAMHG QYSMKSDIYS FGVLVLEIIS GKKNSRAYQM DETSTPGNLV
TYAWRLWRNG SPLELVDPAI GRNYQSNEVT RCIHIALLCV QENPEDRPML STIILMLTSN
TITLPVPRLP SFIPRSRDEL DQISEGLESS QSTGRSVARR ESYENARAFV GIWLELQQIR
FQSEGGFRRA QRCMNRKGNF MPNGTYDVNR RLILSSLPSN VTSKEGLFFN GSIGQEPNRV
YAVGMCIPGS TSDDCSVCIK LASDRLIKNC TNQTNAFAWP ADPTLCHVRY SNTSFLGSAD
LKPRVLLPKE GDIISNLTEF TKTWEDLVVR MIDAASAAKS TPSSSNNHYR ADVAPLTVLQ
NIYALMQCTP DLSSGDCDTC LRQSARAYQS CCGQKQGGVV TRPSCFFRWD LYAFSKAFDN
ITVASLPPPR LPPVASPPPA YDHARTTDNN SKGISSGVVA AITVPTVVTV FILLVLGFVL
CRRRESMQRT EVESDSDIST PQSSQYDFKT VEAATNKFSR HNKLGEGGFG EVYKGTLSNG
TEVAVKRLSE KSGQGIREFK NEAVLVSKLQ HRNLVKLLGF CLEGEEKILI YEFVPNKSLD
YFLFDPEEQD QLHWTQRYKI IGGIARGILY LHQDSQLTVI HRDLKASNIL LDANMNPKIS
DFGLSTIFGM EQTRGNTSRI AGTYGYMSPE YAMQGQYSMK SDIYSFGVLV LEIISGKKNG
GVYQMDETST PGNLVTYAWR LWKNGSPLEM VDLAIGRNYE INEVTRCIHI ALLCVQDNPE
DRPMLSTIIL MLTSNTITLP VPRLPSFIPR SRHELDQVSE GLESSRSTGR YVGHSVNDVS
ITDLEAR
//
