Blast Analysis : gnl|CDD|176901

Analysis	rpsblast_cdd	Start	227
End	360	Strand	+
Length	134	Note	Gaps:8
Hit Coverage	100.00	Hit Length	126
Hit Pident	48.41	E Val	4e-42
Hit Description	cd08892 SRPBCC_Aha1 Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins. This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1 and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones which regulate the dimeric chaperone Hsp90. Hsp90 Aha1 and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90 and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation depending on the client protein for example it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.	Hit Pcons	15.08
Name	Qrob_P0142010.2

1 Protein

Protein Identifier	Organism . Name	Score	Score Type	Protein Description	Alias (in v1)	Code Enzyme	Gene Prediction Quality
Qrob_P0142010.2	Quercus robur	40.3	egn	(M=1) PTHR13009//PTHR13009:SF0 - HEAT SHOCK PROTEIN 90 (HSP90) CO-CHAPERONE AHA-1 // SUBFAMILY NOT NAMED			validated

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