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Database: UniProt
Entry: A0A0D3B427_BRAOL
LinkDB: A0A0D3B427_BRAOL
Original site: A0A0D3B427_BRAOL 
ID   A0A0D3B427_BRAOL        Unreviewed;       573 AA.
AC   A0A0D3B427;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=106334794 {ECO:0000313|EnsemblPlants:Bo3g024060.1};
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:Bo3g024060.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo3g024060.1, 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:Bo3g024060.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily.
CC       {ECO:0000256|ARBA:ARBA00006485}.
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DR   RefSeq; XP_013628614.1; XM_013773160.1.
DR   AlphaFoldDB; A0A0D3B427; -.
DR   STRING; 109376.A0A0D3B427; -.
DR   EnsemblPlants; Bo3g024060.1; Bo3g024060.1; Bo3g024060.
DR   GeneID; 106334794; -.
DR   Gramene; Bo3g024060.1; Bo3g024060.1; Bo3g024060.
DR   KEGG; boe:106334794; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_000288_78_0_1; -.
DR   OMA; YWRKYKL; -.
DR   OrthoDB; 10753at2759; -.
DR   Proteomes; UP000032141; Chromosome C3.
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; cd07840; STKc_CDK9_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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF358; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 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   3: Inferred from homology;
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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          103..388
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          14..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   573 AA;  63562 MW;  6FEA4BA80D151571 CRC64;
     MGCVLCKNSA GAKDEPLPGN LRRDTKTDHL PSSVSVPEVV DIGERKKSQI QTARTWHTGD
     FSGGSSRRTL RMSLSAPEGW PPWLLAACGE SIKDFTPRRA TTYEKLDKIG QGTYSNVYKA
     KDLLTGDIVA LKKVRFDNLE AESVKFMARE ILMLRRLDHP NVIKLQGLVA SRVSCSLYLV
     FEYMDHDLTG LAATQGSKFD ISQVKCFMKQ LLSGLEHCHS RGVLHRDIKG SNLLIDNNGI
     LKIADFGLAT FYDPKQKKQT MTSRVVTLWY RPPELLLGAT NYGTGVDLWS AGCIMAELLA
     GKPVMPGRTE VEQLHKIFKL CGSPSDLYWR KYKLPNATLF KPQHPYKRCV SEAFSGFAPS
     TVHLVETLLA IDPDDRGTST SALNSEFFTS EPLACDPSSL PKYPPSKELN IKLRDQEARR
     QKSLAKKANG VEGARRIRFR GDRTGRAFPA PEANAENQAT LDRCRVLPHT NGKSKSEKFP
     PPHQDGAVGQ HPVEEDHHQS KKSSVFSATH EASFGSSRSL KVGEGTSSMR KISNKDGSSS
     SRKYIWGLKP PPALGLSMDL LFRSRSEVFG VRR
//
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