ID A0A0D3E750_BRAOL Unreviewed; 669 AA.
AC A0A0D3E750;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=106313495 {ECO:0000313|EnsemblPlants:Bo9g068180.1};
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:Bo9g068180.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g068180.1, 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:Bo9g068180.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR RefSeq; XP_013606762.1; XM_013751308.1.
DR AlphaFoldDB; A0A0D3E750; -.
DR STRING; 109376.A0A0D3E750; -.
DR EnsemblPlants; Bo9g068180.1; Bo9g068180.1; Bo9g068180.
DR GeneID; 106313495; -.
DR Gramene; Bo9g068180.1; Bo9g068180.1; Bo9g068180.
DR KEGG; boe:106313495; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR OMA; LLHANTY; -.
DR OrthoDB; 1218670at2759; -.
DR Proteomes; UP000032141; Chromosome C9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
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; PTHR27006:SF554; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE ISOFORM 1; 1.
DR PANTHER; PTHR27006; PROMASTIGOTE SURFACE ANTIGEN PROTEIN PSA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..669
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002260356"
FT TRANSMEM 287..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..144
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 150..255
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 352..632
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 642..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 669 AA; 75212 MW; 8007A4A6489EEB0A CRC64;
MAGSCSSNRP QDLFISFFFF FFLFLPFLSF AQEPVVNVNG SVWDFPSHSS SSSPQSTFSK
NLNSLVASIP LLHANTYNFY NLSVGDISDQ DRVEAIGVCN RVVTSVDCRS CVFQAALNLT
SSSQLREGYW RSTNCMFRYS DNPIFGILET NPVFEALNPN KSTGDRDEFI RLQSDLLNRI
RKRAAAGGSK RKYVQGSGPG PNSSTLFGAV MCTPDLSEKD CNDCLIFGFA NATRGRSGLR
WFCPSCSFQI QTNLRFFHLE SEYEPDPPSD QEPGLLHNWS QGVDKTVIIL ATVGSVVGFS
IFVIFLYFIL KRKQRKEKQR HEGKEDVVEN QIIDENVLRL DFDTIRLATD DFSPGNQLGE
GGFGVVYKGV LDSGEEIAVK RLSMKSGQGD NEFINEVSLV AKLHHRNLVR LIGFCLEGQE
RLLIYDLFKN TSLDHFIFDN DRRMVLEWET RYKIIAGVAR GLLYLHEDSR FKVIHRDLKA
SNVLLDDAMY PKISDFGMAK LFDTDQPCQT RFTSRVAGTY GYMAPEYAMN GKFSVKTDVF
SFGVLVLEIV TGKRNNWSPE DKSSLFLLSY VWKNWREGRV LNIVDPSLIQ TRGLSDEIMK
CIHIGLLCVQ EKAESRPTMA SVVLMLNASS FTLLRPSQPG FYPGDGESTS SSPPTMTLNS
VTITKVDPR
//