ID A0A0D3ALU9_BRAOL Unreviewed; 696 AA.
AC A0A0D3ALU9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN Name=106327437 {ECO:0000313|EnsemblPlants:Bo2g037660.1};
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:Bo2g037660.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo2g037660.1, 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:Bo2g037660.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR RefSeq; XP_013621043.1; XM_013765589.1.
DR AlphaFoldDB; A0A0D3ALU9; -.
DR STRING; 109376.A0A0D3ALU9; -.
DR EnsemblPlants; Bo2g037660.1; Bo2g037660.1; Bo2g037660.
DR GeneID; 106327437; -.
DR Gramene; Bo2g037660.1; Bo2g037660.1; Bo2g037660.
DR KEGG; boe:106327437; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR OMA; TENMERI; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000032141; Chromosome C2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF133; HEAT SHOCK PROTEIN 90-2-RELATED; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 27..182
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 79723 MW; 37D3AF2BBE5B1024 CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KTNNTLTIVD SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VADKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGESLGR GTKMTLHLKE
DQLEYLEERR LKDLVKKHSE FISYHISLWV EKTVEKEISD DEDEEEKKDE EGNVEEVDEE
KEKKKKKIKE VSHEWELVNK QKPIWMRKPE EITKEEYAAF YKSLSNDWEE HLAVKHFSVE
GQLEFKALLF VPKRAPFDLF DTKKKPNNIK LYVRRVFIMD NCEDIIPEWL GFVKGIVDSE
DLPLNISRET LQQNKILKVI RKNLVKKCLE LFFEIAENNE DYNKFYEAFS KNLKLGIHED
SQNRTKIAEL LRYHSTKSGD ELTSLKDYVT RMKEGQNDIF YITGESKKAV ENSPFLEKLK
KKGYEVLYMV DAIDEYAIGQ LKEFEGKKLV SATKEGLKLD ESEDEKKKKE ELKEKFEGLC
KVIKDILGDK VEKVIVSDRV VDSPCCLVTG EYGWTANMER IMKAQALRDS SMAGYMSSKK
TMEINPENAI MEELRKRAEA DKNDKSVKDL VLLLFETALL TSGFSLDEPN TFGNRIHRML
KLGLSIDEDD AVEADAEMPP LEDDADAEGS KMEEVD
//