ID I1I8C4_BRADI Unreviewed; 699 AA.
AC I1I8C4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN Name=100840035 {ECO:0000313|EnsemblPlants:PNT68367};
GN ORFNames=BRADI_3g39620v3 {ECO:0000313|EMBL:KQJ98867.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:PNT68367};
RN [1] {ECO:0000313|EMBL:KQJ98867.1, ECO:0000313|EnsemblPlants:PNT68367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98867.1,
RC ECO:0000313|EnsemblPlants:PNT68367};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ98867.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98867.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT68367}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT68367};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CM000882; KQJ98867.1; -; Genomic_DNA.
DR EMBL; CM000882; PNT68367.1; -; Genomic_DNA.
DR RefSeq; XP_010235286.1; XM_010236984.2.
DR AlphaFoldDB; I1I8C4; -.
DR STRING; 15368.I1I8C4; -.
DR EnsemblPlants; KQJ98867; KQJ98867; BRADI_3g39620v3.
DR EnsemblPlants; PNT68367; PNT68367; BRADI_3g39620v3.
DR GeneID; 100840035; -.
DR Gramene; KQJ98867; KQJ98867; BRADI_3g39620v3.
DR Gramene; PNT68367; PNT68367; BRADI_3g39620v3.
DR KEGG; bdi:100840035; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; I1I8C4; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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:SF99; HISTIDINE KINASE_HSP90-LIKE ATPASE DOMAIN-CONTAINING PROTEIN; 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:UP000008810}.
FT DOMAIN 28..182
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 214..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 80177 MW; CB44AFD561FCC3E1 CRC64;
MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA
QPELFIHIVP DKATNTLTLI DSGIGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG
QFGVGFYSAY LVADRVVVTT KHNDDEQYVW ESQAGGSFTV TRDTGESLGR GTKMTLYLKE
DQLEYLEERR LKDLVKKHSE FISYPISLWT EKTTEKEISD DEDEEEKKDT EEGKVEEIDE
EKEEKEKKKK TIKEVSHEWS LINKQKPIWM RKPEEITKEE YAAFYKSLTN DWEEHLAVKH
FSVEGQLEFK AVLFVPKRAP FDLFDTRKKA NNIKLYVRRV FIMDNCEELI PEWLGFVKGI
VDSEDLPLNI SRETLQQNKI LKVIRKNLVK KSIELFFEIA ENKEDYNKFY ESFSKNLKLG
IHEDSANRTK IAELLRYHST KSGDELTSLK DYVTRMKEGQ NDIYYITGES KKAVENSPFL
ERLKKKGYEV IYMVDAIDEY AIGQLKEFEG KKLVSATKEG LKLEDSEDEK KKKEELKEKF
EGLCKVIKDV LGDRVEKVIV SDRVVDSPCC LVTGEYGWTA NMERIMKAQA LRDSSMGGYM
SSKKTMEINP ENAIMEELRK RADADKNDKS VKDLVMLLFE TSLLTSGFSL DDPNTFGTRI
HRMLKLGLSI DEDETAEADD TDMPALEDDA GESKMEEVD
//
