ID   C1IZ10_9STRA            Unreviewed;       366 AA.
AC   C1IZ10;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ACM78551.1};
DE   Flags: Fragment;
GN   Name=hsp90 {ECO:0000313|EMBL:ACM78551.1};
OS   Thraustochytrium aureum.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC   Thraustochytrida; Thraustochytriaceae; Thraustochytrium.
OX   NCBI_TaxID=42467 {ECO:0000313|EMBL:ACM78551.1};
RN   [1] {ECO:0000313|EMBL:ACM78551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 34304 {ECO:0000313|EMBL:ACM78551.1};
RX   PubMed=19213601; DOI=10.1016/j.protis.2008.11.004;
RA   Riisberg I., Orr R.J., Kluge R., Shalchian-Tabrizi K., Bowers H.A.,
RA   Patil V., Edvardsen B., Jakobsen K.S.;
RT   "Seven gene phylogeny of heterokonts.";
RL   Protist 160:191-204(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; FJ030914; ACM78551.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1IZ10; -.
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; IPR003594; HATPase_C.
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   SMART; SM00387; HATPase_c; 1.
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:ACM78551.1}.
FT   DOMAIN          4..159
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          194..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..212
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACM78551.1"
FT   NON_TER         366
FT                   /evidence="ECO:0000313|EMBL:ACM78551.1"
SQ   SEQUENCE   366 AA;  42026 MW;  78E1A97B703CEF4C CRC64;
     FYSNKEIFPR ELISNASDAL DKVRYQSITD PSVLEHEEKM EIKIVPDKAN NTLTLIDTGL
     GMTKADLVNN LGTIAKSGTK AFMEALSAGA DISMIGQFGV GFYSAYLVAD KVEVHSKHND
     DEQHVWSSSA GGSFSVAKDT DYERIGRGTH IVLHLKEDML EFLEERRIKD LVKKHSEFIG
     FDIFLMVEKS VDKEVTDDEE EEEEEGDEDK PKVEDVTDDK EGDKERKKKT KKITEVQHEW
     EKLNATKPIW MRKPEEITSE EYASFYKSLT NDWEEPLSTK HFSVEGQLEF RALLFVPKRA
     PFDMFEGGKK KSNSIKLYVR RVFIMDNCED LMPEYLSFVR GLVDSEDLPL NISREMLQQN
     KILKVI
//