ID   E9LJ30_9STRA            Unreviewed;       362 AA.
AC   E9LJ30;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ADP21674.1};
DE   Flags: Fragment;
GN   Name=HSP90 {ECO:0000313|EMBL:ADP21674.1};
OS   Phytophthora thermophila.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=880414 {ECO:0000313|EMBL:ADP21674.1};
RN   [1] {ECO:0000313|EMBL:ADP21674.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VHS16164 {ECO:0000313|EMBL:ADP21674.1};
RX   PubMed=22025801; DOI=.3767/003158511X557577;
RA   Jung T., Stukely M.J., Hardy G.E., White D., Paap T., Dunstan W.A.,
RA   Burgess T.I.;
RT   "Multiple new Phytophthora species from ITS Clade 6 associated with natural
RT   ecosystems in Australia: evolutionary and ecological implications.";
RL   Persoonia 26:13-39(2011).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; HQ012919; ADP21674.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9LJ30; -.
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:ADP21674.1}.
FT   REGION          151..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..175
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADP21674.1"
FT   NON_TER         362
FT                   /evidence="ECO:0000313|EMBL:ADP21674.1"
SQ   SEQUENCE   362 AA;  41590 MW;  C4E08A9993B1C299 CRC64;
     EIKVIPDKAN GTLTIQDSGI GMTKADLINN LGTIAKSGTK AFMEALAAGA DISMIGQFGV
     GFYSAYLVAD KVVVHSKHND DEQYVWESAA GGSFTVTPDT TEPILRGTRI VLKLKEDMLE
     YLEERKLKDL VKKHSEFIGF PIKLYVEKTE EKEVTDDEEE EDEKEGEDDK PKVEEVEDEE
     GEKKKKTKKI KEVTHEWDHL NSQKPIWMRK PEDVTHEEYA SFYKSLTNDW EEHAAVKHFS
     VEGQLEFKAC LFTPKRAPFD MFEGGAKKKI NNIKLYVRRV FIMDNCEELM PEYLSFVKGV
     VDSEDLPLNI SRETLQQNKI LRVIKKNLVK KCLEMFAELA EDNEKYQKFY EAFSKNLKLG
     IH
//