ID   E0XJK6_9NEOP            Unreviewed;       716 AA.
AC   E0XJK6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
GN   Name=HSP90 {ECO:0000313|EMBL:ADM26739.1};
OS   Exangerona prattiaria.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC   Geometridae; Ennominae; Exangerona.
OX   NCBI_TaxID=876857 {ECO:0000313|EMBL:ADM26739.1};
RN   [1] {ECO:0000313|EMBL:ADM26739.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu P., Li T., Huang D.W.;
RT   "Identification of conserved nucleotide sequences within 3'UTR region of
RT   the cytoplasmic HSP90: design of PCR primers for amplification of HSP90
RT   from Lepidoptera.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; GU230736; ADM26739.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0XJK6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.40.50.11260; -; 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: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   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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:ADM26739.1}.
FT   DOMAIN          35..189
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          222..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  82404 MW;  56EF4A0082746AE2 CRC64;
     MPEEMETQSG DVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNSSDA LDKIRYESLT
     DPSKLDSGKE LYIKIIPNKS EGTLTIIDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG
     ADISMIGQFG VGFYSCYLVA DRVTVHSKHN DDEQYVWESA AGGSFTVRPD HGEPLGRGTK
     IILHVKEDLA EFMEEHKVKE VVKKHSQFIG YPIKLLVEKE REKELSDDEA EEEKKEDDKD
     EKPKIEDVGE DEEEDKKDKK KKKTIKEKYT EDEELNKTKP IWTRNADDIT QEEYGDFYKS
     LTNDWEDHLA VKHFSVEGQL EFRALLFVPR RAPFDLFENK KRKNNIKLYV RRVFIMDNCE
     DLIPEYLNFI RGVVDSEDLP LNISREMLQQ NKILKVIRKN LVKKCLELFE ELAEDKENYK
     KYYEQFSKNL KLGIHEDSQN RSKLADLLRF HTSASGDEAC SLKEYVSRVK ENQKHIYYIT
     GENRDQVSNS SFVERVKKRG YEVVYMTEPI DEYVVQQMRE YDGRTLVSVT KEGLELPEDE
     EEKKKREEDK VKFEGLCKVM KNILDNKVEK VVVSNRLVES PCCIVTAQYG WSANMERIMK
     AQALRDTSTM GYMAAKKHLE INPDHSIVET LRQKSEADKN DKAVKDLVIL LYETALLSSG
     FTLDEPQVHA SRIYRMIKLG LGIDEDEPIQ IEESSAGDVP PLEGDADDAS RMEEVD
//