1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR019805 | Conserved_site | Heat shock protein Hsp90, conserved site |
1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR003594 | Domain | Histidine kinase-like ATPase, C-terminal domain |
| Type: | Domain | Name: | Heat shock protein Hsp90, N-terminal |
| Description: | Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) []. The 90 kDa heat shock protein, Hsp90, is one of the most abundant proteins in eukaryotic cells, comprising 1-2% of cellular proteins under non-stress conditions []. Its contribution to various cellular processes including signal transduction, protein folding, protein degradation and morphological evolution has been extensively studied [, ]. The full functional activity of Hsp90 is gained in concert with other co-chaperones, playing an important role in the folding of newly synthesised proteins and stabilisation and refolding of denatured proteins after stress. Apart from its co-chaperones, Hsp90 binds to an array of client proteins, where the co-chaperone requirement varies and depends on the actual client. The sequences of hsp90s show a distinctive domain structure, with a highly-conserved N-terminal domain separated from a conserved, acidic C-terminaldomain by a highly-acidic, flexible linker region. | Short Name: | Hsp90_N |
| DB identifier | Type | Name |
|---|---|---|
| IPR019805 | Conserved_site | Heat shock protein Hsp90, conserved site |
| DB identifier | Type | Name |
|---|---|---|
| IPR003594 | Domain | Histidine kinase-like ATPase, C-terminal domain |
