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Database: UniProt
Entry: A0A0D3C570_BRAOL
LinkDB: A0A0D3C570_BRAOL
Original site: A0A0D3C570_BRAOL 
ID   A0A0D3C570_BRAOL        Unreviewed;       383 AA.
AC   A0A0D3C570;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=106339789 {ECO:0000313|EnsemblPlants:Bo4g188360.1};
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:Bo4g188360.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo4g188360.1, 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:Bo4g188360.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   RefSeq; XP_013634116.1; XM_013778662.1.
DR   AlphaFoldDB; A0A0D3C570; -.
DR   STRING; 109376.A0A0D3C570; -.
DR   EnsemblPlants; Bo4g188360.1; Bo4g188360.1; Bo4g188360.
DR   GeneID; 106339789; -.
DR   Gramene; Bo4g188360.1; Bo4g188360.1; Bo4g188360.
DR   KEGG; boe:106339789; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_21_1_1; -.
DR   OMA; NTEIHAG; -.
DR   OrthoDB; 2910608at2759; -.
DR   Proteomes; UP000032141; Chromosome C4.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd14066; STKc_IRAK; 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; PTHR45621; OS01G0588500 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR45621:SF103; SERINE_THREONINE-PROTEIN KINASE BIK1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          68..357
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          357..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   383 AA;  42860 MW;  AAD468DDFF6C1A3F CRC64;
     MGSCFSSPVK ADNFSYNDKS SYLSGLSMWS RTSSSVRAAA RKTEEEILEL TSVKSFTFNE
     LKLATRNFRP DSVVGEGGFG SVFKGWLDET SLTPTKPGTG LVIAVKKLNQ EGLQGHHEWL
     TEINYLGELS HPNLVKLVGY CLEDDHHLLV YEFMQNGSLE NHLFRRGSHF KPLTWSLRVK
     VALDAAKGLA FLHSDPVKVI YRDFKASNIL LDADYNGKLS DFGLARDGPM GDLSYVSTRV
     MGTYGYAAPE YMSSGHLNSR SDVYSFGVVL LEILTGKEAL DYNRPAEEED LVKWARPYLT
     SKRKVFRIVD PRLDSQYLPE EAVRMASIAV LCISFEPKSR PTMDQVVRAL QQLQDNLGKP
     TQTDTVKDGK RHGSKTRAKL PEV
//
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