The domain within your query sequence starts at position 29 and ends at position 159; the E-value for the Aha1_N domain shown below is 1.59e-54.
ERDATIWSKGKLRELLVGIAMENEAGRCEISELKQVEGEASCNSRKGKLIFFYEWNIKLA WKGTVKESGAKHKGLIEIPSLSEENEINDTEVNVSKKKGDGEILKDLMRTTGTAKVREAL GEYLKALKTGK
Aha1_NActivator of Hsp90 ATPase, N-terminal |
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SMART accession number: | SM01000 |
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Description: | This domain is predominantly found in the protein 'Activator of Hsp90 ATPase', it adopts a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity (PUBMED:15039704). |
Interpro abstract (IPR015310): | This domain is predominantly found N-terminal in the protein Activator of Hsp90 ATPase (Aha1). Aha1 adopts a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two alpha helices are packed together, with the beta-sheet curving around them. The N-terminal domain of Aha1 interacts with Hsp90 and stimulates its ATPase activity [ (PUBMED:15039704) ]. |
GO function: | chaperone binding (GO:0051087), ATPase activator activity (GO:0001671) |
Family alignment: |
There are 2381 Aha1_N domains in 2334 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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