The domain within your query sequence starts at position 15 and ends at position 149; the E-value for the Aha1_N domain shown below is 2.52e-57.

ERDATIWSKGKLRELLVGIAMENEAGRCEISELKQVEGEASCNSRKGKLIFFYEWNIKLA
WKGTVKESGAKHKGLIEIPSLSEENEINDTEVNVSKKKGDGEILKDLMRTTGTAKVREAL
GEYLKALKTEFTTGM

Aha1_N

Activator of Hsp90 ATPase, N-terminal
Aha1_N
SMART accession number:SM01000
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:
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There are 2381 Aha1_N domains in 2334 proteins in SMART's nrdb database.

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