ID A0A078J4C1_BRANA Unreviewed; 911 AA.
AC A0A078J4C1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=BnaA01g35160D protein {ECO:0000313|EMBL:CDY61011.1};
GN Name=BnaA01g35160D {ECO:0000313|EMBL:CDY61011.1};
GN ORFNames=GSBRNA2T00030397001 {ECO:0000313|EMBL:CDY61011.1};
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:CDY61011.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY61011.1, 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).
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DR EMBL; LK033944; CDY61011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078J4C1; -.
DR STRING; 3708.A0A078J4C1; -.
DR PaxDb; 3708-A0A078J4C1; -.
DR EnsemblPlants; CDY61011; CDY61011; GSBRNA2T00030397001.
DR Gramene; CDY61011; CDY61011; GSBRNA2T00030397001.
DR OMA; VDQICEV; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR ExpressionAtlas; A0A078J4C1; baseline.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13999; STKc_MAP3K-like; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44329:SF231; PROTEIN KINASE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF14381; EDR1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 631..889
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 911 AA; 102018 MW; 6E8C42D070C30F51 CRC64;
MPHRTTYFFP RQFPDRGFDP FSHKTDHDKK SSPSVESFGF ESKKPNGGAG DPNKEKEKEE
VVFPSSNSAV SDLLNGLSDD RISEKKQQQQ HLAAFYEWLA EKKAKLSRSS TTTGHVRPTG
HVRPTRISIS SEGDEEREHL LPSSSASDSP DSIVAAAASS SSARTVNINE RNIDRSFDRE
VSLPRMSSES SFAGSFFSGT TVDGNFSSFS SPTEARETST TTRVSVAKEE EREAEVRDES
KEQTLAQKSK EGYYLQVTLA RRLSSQANLG GDSVQIQSTE TISYRFWVSG CLSYSDKIAD
GFYSILGMDP YLWLMCNDSE EGKKLPSLLL LKETEPSDTS MEVVLIDRRE DSRLKEMEDK
AHELYCASEN MLVLVEQLGR LVAVYMGGNF QMEQGDLQKR WKLVSNRLKE FRKCIILPIG
SLTMGLCRHR AILFKKLADY IGLPCRIARG CRYCKENHQS CCLVKIDDEK KLSREYVVDL
IGKPGNVHDP DSTINGGTHS QIPSPLRMSH LTEVSRPFVR STSPFCFTKA SSTVSTESIV
RPALPLDIPK LSEDKTASQE TCKEENSLLE DPVENNVIKQ GNGELPVEQE IAEAETRKDK
KVRLPVDAIS PFLSIEPSLA SDWLEISWDE LHIKERVGAG SFGTVHRAEW HGSDVAVKIL
SIQDFHDDQF REFLREVAIM KRVRHPNVVL FMGAVTDRTR LSIVTEYLPR GSLFRLIHRP
ASGELLDHRR RLRMALDVAK GLNYLHCLNP PVVHWDLKSP NLLVDKNWTV KVCDFGLSRF
KANTFIPSKS VAGTPEWMAP EFLRGEPTNE KSDVYSFGVV LWELITLQQP WNGLSPAQVV
GAVAFQNRRL IIPPNTSPVL VSLMEACWAD EPAQRPAFGG IVDTLKKLLK SPVQLIQMGG
DKGVRDALIS S
//