ID   Q4JH56_9ACAR            Unreviewed;       172 AA.
AC   Q4JH56;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Heat shock protein 82 {ECO:0000313|EMBL:AAY89880.1};
DE   Flags: Fragment;
GN   Name=hsp82 {ECO:0000313|EMBL:AAY89880.1};
OS   Adoristes poppei.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Oribatida; Brachypylina; Gustavioidea;
OC   Liacaridae; Adoristes.
OX   NCBI_TaxID=229811 {ECO:0000313|EMBL:AAY89880.1};
RN   [1] {ECO:0000313|EMBL:AAY89880.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Domes K., Norton R.A., Schmidt H., Scheu S., Maraun M.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; DQ090788; AAY89880.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JH56; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:AAY89880.1}.
FT   REGION          85..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY89880.1"
FT   NON_TER         172
FT                   /evidence="ECO:0000313|EMBL:AAY89880.1"
SQ   SEQUENCE   172 AA;  20286 MW;  4254D2EB05E7DCF2 CRC64;
     SAYLIADKVT VTSKHNDDEQ YIWESSAGGS FTIKVDNSEP LGRGTKIVLH LKEDQLEYSE
     EKRIKEIVKR HSQFIGYPIK LVVQKEREKE VSDDEEEKEE KDDEKKDEEE KKEGGDEEEA
     KVEDVEDSDE KKDKKKKKKI KEKYIEDEEL NKTKPIWMRN PDDITQEEYG EF
//