ID   J7IME0_9NEOP            Unreviewed;       182 AA.
AC   J7IME0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Heat shock protein 90kDa {ECO:0000313|EMBL:AFQ40764.1};
DE   Flags: Fragment;
OS   Heliconius timareta ssp. n. CPD-2012.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Heliconiinae; Heliconiini; Heliconius.
OX   NCBI_TaxID=1207008 {ECO:0000313|EMBL:AFQ40764.1};
RN   [1] {ECO:0000313|EMBL:AFQ40764.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22737081; DOI=10.1371/journal.pgen.1002752;
RA   Pardo-Diaz C., Salazar C., Baxter S.W., Merot C., Figueiredo-Ready W.,
RA   Joron M., McMillan W.O., Jiggins C.D.;
RT   "Adaptive Introgression across Species Boundaries in Heliconius
RT   Butterflies.";
RL   PLoS Genet. 8:E1002752-E1002752(2012).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; JX004710; AFQ40764.1; -; Genomic_DNA.
DR   EMBL; JX004711; AFQ40765.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7IME0; -.
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:AFQ40764.1}.
FT   REGION          122..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFQ40764.1"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|EMBL:AFQ40764.1"
SQ   SEQUENCE   182 AA;  20709 MW;  9FF4B6CAA8598CDF CRC64;
     NNLGTIAKSG TKAFTEALQA GADISMIGQF GVGFYSCYLV ADRVTVHSKH NDDEQYMWES
     AAGGSFTVRS DPGEPLGRGT KIVLHVKEDL AEFMEEHKVK EIVKKHSQLI GYPIKLVIEK
     EREKELSDDE AEEEKKEDEK EDEKPKIEDV GEDEDEDNKD KKKKKKTIKE KYTEDEELNK
     TK
//