ID A0A0D3E887_BRAOL Unreviewed; 792 AA.
AC A0A0D3E887;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
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:Bo9g077990.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g077990.1, 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:Bo9g077990.1}
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 AlphaFoldDB; A0A0D3E887; -.
DR EnsemblPlants; Bo9g077990.1; Bo9g077990.1; Bo9g077990.
DR Gramene; Bo9g077990.1; Bo9g077990.1; Bo9g077990.
DR eggNOG; ENOG502SE86; Eukaryota.
DR HOGENOM; CLU_354656_0_0_1; -.
DR OMA; FHEGIRE; -.
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 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27002:SF994; (RAPE) HYPOTHETICAL PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..792
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002260452"
FT DOMAIN 19..128
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 368..711
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 792 AA; 89682 MW; 28FA5A61B7259DAC CRC64;
MENFSNVILF SCFLLLLTFI DAKTVCEGSL FSDNSTYSDN LNSLFSSLAS NVVANDGFYN
TSIGEGTNKV YGLALCGRGY EKQACVNCVE QGIQDLEDIC PNRIKSFKWT TRDSDNASCL
VRYANYSVFE KLELFPPAPE NSSVVLKYYS VVRAEFTEFA DVYMMMKCTP DILPSECNIC
FMQCVLNFQN NNWGRQGGAG KLLSCCFRWD LYNIPRSSEN MTRVSMISRG STPPREDTEL
KPGYDEKGMA SSSGNKKYPP RLYEIYGHRI EEAEVPLLSW HDSHQRLSDQ INRSYQQCDR
IWLQRFMMRK KDSEWNYRYN CGSTLFIIFD QRRKSYNKNI SESECCDSDG QSMLRFGLAM
ILSVTNDFSP ENKLGQGGFG TVYKGVLPNG QEIAVKRLVS GSGQGGDEEI LVYELVPNSS
LEHFIFDEEK RLLLTWEVTF KIIEGVARGL LYLHEDSQLK IIHRDLKASN ILLDSEMNPK
VADFGTARLF EADETRAETR LNSWNPLPGL PPQPPGFPPS SPEFSKFEKF LVDCFLWCAC
LGPGTLPPLE IGLIDCVLLW SLSWKRADNR KLSRFSPYDR GYDEPNNNRR HDHQSRERHN
HSDLRDFHEG IRENKRDGNY HSRHYSSSED REGNRSNRPA SDRLPPIRES SYVSSRPQGM
RTANPASKGY WRPVSGDGAR GQSNSIQSQV SHTPSPRTQR EPMILDGNPP LASPQTPRVS
NNSGERRSAL ERLSGAPDRV PLLQNGVANS DSGRLQEVNV QYLEDALPYQ TPPELMRPSS
SKAAGGSLHI LR
//
