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Database: UniProt
Entry: A0A0D3D297_BRAOL
LinkDB: A0A0D3D297_BRAOL
Original site: A0A0D3D297_BRAOL 
ID   A0A0D3D297_BRAOL        Unreviewed;       572 AA.
AC   A0A0D3D297;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Non-specific serine/threonine protein kinase {ECO:0000313|EnsemblPlants:Bo7g003540.1};
GN   Name=106304454 {ECO:0000313|EnsemblPlants:Bo7g003540.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo7g003540.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo7g003540.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo7g003540.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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DR   RefSeq; XP_013596316.1; XM_013740862.1.
DR   AlphaFoldDB; A0A0D3D297; -.
DR   STRING; 109376.A0A0D3D297; -.
DR   EnsemblPlants; Bo7g003540.1; Bo7g003540.1; Bo7g003540.
DR   GeneID; 106304454; -.
DR   Gramene; Bo7g003540.1; Bo7g003540.1; Bo7g003540.
DR   KEGG; boe:106304454; -.
DR   eggNOG; KOG0605; Eukaryota.
DR   HOGENOM; CLU_000288_67_0_1; -.
DR   OMA; IRSHEWY; -.
DR   OrthoDB; 988261at2759; -.
DR   Proteomes; UP000032141; Chromosome C7.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd21742; MobB_NDR_LATS-like; 1.
DR   CDD; cd05599; STKc_NDR_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF342; AGC (CAMP-DEPENDENT, CGMP-DEPENDENT AND PROTEIN KINASE C) KINASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          124..423
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          424..496
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   572 AA;  65041 MW;  ADC83E618F36421C CRC64;
     MDSAKGWFQK RQMRGGSRYK GGSGGGGGGS NGSADEQPNV ETDEEAVSNT TKQKVAAAKQ
     YIENHYKEQM KILQERKERR SLLEQKLADA DVCEEDQNNL LKFLEKKETE YMRLQRHKLG
     VADFDLLTMI GKGAFGEVRI CKEKTTGQVY AMKKLKKAEM LRRGQVEHVR AERNLLAEVD
     SNYIVKLYCS FQDDDHLYLV MEYLPGGDMM TLLMRKDTLT EEEAKFYVAE TVLAVESIHR
     HNYIHRDIKP DNLLLDRYGH LRLSDFGLCK PLDCSAIGEN EFSNNPNNGS TTEQEGGSGA
     PKRTQQEQLE HWQKNRRKLA YSTVGTPDYI APEVLLKKGY GMECDWWSLG AIMYEMLVGY
     PPFYADDPMS TCRKIVNWKS HLKFPEEAVL SREAKDLINS LLCSVRRRLG SKGADEIKAH
     PWFETVDWDT IFDMDAAFVP EVNDDLDTQN FEKFDESESQ TETSSKSGPW RKMLSSKDIN
     FVGYTYKNFE IVNDYQVPGM AELKKKNKSK RPPMVKSLFD GGSSETSDSP EATTRSAGDR
     PPPIPPVVQG SFLKLLPPEL EVRPKQEESE AC
//
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