The domain within your query sequence starts at position 44 and ends at position 218; the E-value for the GrpE domain shown below is 1.8e-42.

SSEDPPDGLGPSLAEQALRLKAVKLEKEVQDLTLRYQRAVADCENIRRRTQRCVEDAKIF
GIQSFCKDLVEVADILEKTAKCCSEGAEPEDHRRTLEKVFQGLSLLEARLKSVFTKHGLE
KMTPIGDKYDPHEHELICHMPAGVGVQPGTVALVRQDGYKLHGRTIRLAQVEVAV

GrpE

 GrpE
PFAM accession number:PF01025
Interpro abstract (IPR000740):

Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolysing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. In prokaryotes the dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold [ (PUBMED:8280473) ]. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins: unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle [ (PUBMED:14984054) (PUBMED:20036249) (PUBMED:22544739) (PUBMED:11580258) (PUBMED:12369934) (PUBMED:10430558) (PUBMED:22683810) (PUBMED:24269840) (PUBMED:19075746) ].

In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.

The X-ray crystal structure of GrpE in complex with the ATPase domain of DnaK revealed that GrpE is an asymmetric homodimer, bent in a manner that favours extensive contacts with only one DnaK ATPase monomer [ (PUBMED:15136046) ]. GrpE does not actively compete for the atomic positions occupied by the nucleotide. GrpE and ADP mutually reduce one another's affinity for DnaK 200-fold, and ATP instantly dissociates GrpE from DnaK.

GO process:protein folding (GO:0006457)
GO function:protein homodimerization activity (GO:0042803), chaperone binding (GO:0051087), adenyl-nucleotide exchange factor activity (GO:0000774)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GrpE