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Database: UniProt
Entry: A0A0D3EEB5_BRAOL
LinkDB: A0A0D3EEB5_BRAOL
Original site: A0A0D3EEB5_BRAOL 
ID   A0A0D3EEB5_BRAOL        Unreviewed;       518 AA.
AC   A0A0D3EEB5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=106318018 {ECO:0000313|EnsemblPlants:Bo9g154710.1};
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:Bo9g154710.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo9g154710.1, 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:Bo9g154710.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
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DR   RefSeq; XP_013611302.1; XM_013755848.1.
DR   AlphaFoldDB; A0A0D3EEB5; -.
DR   STRING; 109376.A0A0D3EEB5; -.
DR   EnsemblPlants; Bo9g154710.1; Bo9g154710.1; Bo9g154710.
DR   GeneID; 106318018; -.
DR   Gramene; Bo9g154710.1; Bo9g154710.1; Bo9g154710.
DR   KEGG; boe:106318018; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_21_0_1; -.
DR   OMA; KKFAQMA; -.
DR   OrthoDB; 2999496at2759; -.
DR   Proteomes; UP000032141; Chromosome C9.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47985; OS07G0668900 PROTEIN; 1.
DR   PANTHER; PTHR47985:SF4; SERINE_THREONINE-PROTEIN KINASE PBL27; 1.
DR   Pfam; PF00069; Pkinase; 1.
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:UP000032141};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          85..362
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   518 AA;  56159 MW;  E717DEB3D54798E9 CRC64;
     MSGCLPCFGS SAKDAASKDS VKKEASAKAK DASVTQSHHV SLDKSKSKGG SEQKKELTAP
     KEGPTAHIAA QTFTFRELAA ATKNFRPDCL LGEGGFGRVY KGRLETTGQI VAVKQLDRNG
     LQGNREFLVE VLMLSLLHHT NLVNLIGYCA DGDQRLLVYE YMPLGSLEDH LHDLPPDKES
     LDWNTRMTIA AGAAKGLEYL HDKANPPVIY RDLKSSNILL GDGYHPKLSD FGLAKLGPVG
     DKTHVSTRVM GTYGYCAPEY AMTGQLTLKS DVYSFGVVFL ELITGRKAID NARAHGEHNL
     VAWARPLFKD RRKFPKMADP SLQGRYPMRG LYQALAVAAM CLQEQAATRP LIGDVVTALT
     YLASQTFDPN AASSQNSRSG SGGGGPPFIR TRDERRSMGD GSSLDSPAET RSRLGSPATH
     KNSPDYRRRD MVREVNAGSE AGSENGGGSG RKWGLSDVEG TESQRGSPAS VGRGTRGTPR
     NRDLDRERAV AEAKVWGENW RERKRGINGP GSFDSSND
//
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