ID   Q86LJ9_9EUKA            Unreviewed;       360 AA.
AC   Q86LJ9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:AAO46124.1};
DE   Flags: Fragment;
OS   Streblomastix strix.
OC   Eukaryota; Metamonada; Preaxostyla; Oxymonadida; Streblomastigidae;
OC   Streblomastix.
OX   NCBI_TaxID=222440 {ECO:0000313|EMBL:AAO46124.1};
RN   [1] {ECO:0000313|EMBL:AAO46124.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12595248; DOI=10.1016/S0022-2836(03)00057-3;
RA   Keeling P.J., Leander B.S.;
RT   "Characterisation of a non-canonical genetic code in the oxymonad
RT   Streblomastix strix.";
RL   J. Mol. Biol. 326:1337-1349(2003).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; AY188867; AAO46124.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86LJ9; -.
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   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
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   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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:AAO46124.1}.
FT   REGION          176..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAO46124.1"
FT   NON_TER         360
FT                   /evidence="ECO:0000313|EMBL:AAO46124.1"
SQ   SEQUENCE   360 AA;  41692 MW;  3DDFF71F739B1AF4 CRC64;
     SNASDALDKI RYESLTNKAV LDSEPKMEIR IVPDKVNKVL HIIDTGIGMT RADLVNNLGT
     IANSGTKAFM EAIQAGADVS MIGQFGVGFY SAYLVAQNVL VTSKHNDDEQ YIWESAAGDS
     FTIREDKEGE KLLRGTKISL FLKDDQLEFL EEHKIKELVK KHSEFISYPI ALQTEKTVEK
     EVEEEEEEEE EKKGEKKEEE KKEEKKEGEE EKKKEGEEDE PKVEEEKKKK DKKKRKVTEV
     THDYEQLNKT KAIWMRKPEE ITKEEYAAFY KSISNDWEDH LSVKHFSFEG SLEFRAVLFC
     PRRAPFDMFE TKKKNTNVKL YVRRVLIMEN CEELIPEYLG FIKGVVDSED LPLNISRETL
//