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Database: UniProt
Entry: A0A078G8H8_BRANA
LinkDB: A0A078G8H8_BRANA
Original site: A0A078G8H8_BRANA 
ID   A0A078G8H8_BRANA        Unreviewed;       547 AA.
AC   A0A078G8H8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=BnaA09g44420D {ECO:0000313|EMBL:CDY21691.1};
GN   ORFNames=DARMORV10_A09P59610.1 {ECO:0000313|EMBL:CAF2050230.1},
GN   GSBRNA2T00016183001 {ECO:0000313|EMBL:CDY21691.1};
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:CDY21691.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY21691.1, 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).
RN   [2] {ECO:0000313|EMBL:CDY21691.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2050230.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; HG994363; CAF2050230.1; -; Genomic_DNA.
DR   EMBL; LK032123; CDY21691.1; -; Genomic_DNA.
DR   RefSeq; XP_013643392.1; XM_013787938.1.
DR   RefSeq; XP_013664631.1; XM_013809177.1.
DR   STRING; 3708.A0A078G8H8; -.
DR   PaxDb; 3708-A0A078G8H8; -.
DR   EnsemblPlants; CDY21691; CDY21691; GSBRNA2T00016183001.
DR   GeneID; 106369077; -.
DR   Gramene; CDY21691; CDY21691; GSBRNA2T00016183001.
DR   KEGG; bna:106369077; -.
DR   OMA; FEERDAF; -.
DR   OrthoDB; 655312at2759; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 2.
DR   CDD; cd05117; STKc_CAMK; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24349:SF420; (RAPE) HYPOTHETICAL PROTEIN; 1.
DR   PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
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}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..323
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          366..401
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          402..437
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          438..473
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          474..509
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   547 AA;  61921 MW;  ED7A9C6FBAB027F1 CRC64;
     MGNCNVCVRP PNPEESKPTP KPKKTNQNRK LNPFTSDFIR SPVRTRAPKD AVIPTSHQTK
     ITDKYILGRE LGRGEFGITY LCTDRESREA LACKSISKRK LRTAVDVEDV RREVSIMSTL
     PDHPNVVKLR ATYEDGENVH LVMELCEGGE LFDRIVARGH YTERAAAGVA RTIAEVVMMC
     HVNGVVHRDL KPENFLFANK KENSALKAID FGLSVFFKPG EKFKEIVGSP YYMAPEVLKR
     DYGPEVDVWS AGVIIYILLC GVPPFWAETE QGVALAILRG VIDFKRDPWP QISESAKSLV
     RQMLNPDPTK RLTAQQVLAH PWVQNAKKAP NVPLGDIVRS RLKQFSMMNR FKKKVLRVIA
     EHLSIQEVEV IKDMFSLMDE DNDGRITYLE LKAGLQKVGS QLGEPEIKML MEVADVDGNG
     FLDYGEFVAV IIHLQKIEND ELFKLAFMFF DKDGSTYIEL DELREALTDE LGEPDVSVLN
     DIMREVDSDK DGRINYDEFV TMMKAGTDWR KASRQYSRER FKSLSINLMK DGSLHLHDAL
     TGQSVPV
//
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