The domain within your query sequence starts at position 690 and ends at position 814; the E-value for the HSP70 domain shown below is 1.2e-6.



PFAM accession number:PF00012
Interpro abstract (IPR013126):

Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region [ (PUBMED:9476895) ].

Hsp70 proteins have an average molecular weight of 70kDa [ (PUBMED:2686623) (PUBMED:2944601) (PUBMED:3282176) ]. In most species, there are many proteins that belong to the Hsp70 family. Some of these are only expressed under stress conditions (strictly inducible), while some are present in cells under normal growth conditions and are not heat-inducible (constitutive or cognate) [ (PUBMED:2143562) (PUBMED:2841196) ]. Hsp70 proteins can be found in different cellular compartments(nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example).

This entry represents the Hsp70 family, and includes chaperone protein DnaK and luminal-binding proteins. It also includes heat shock protein 110 (Hsp110) from Caenorhabditis elegans which helps prevent the aggregation of denatured proteins in neurons [ (PUBMED:19165329) ]. Also included is endoplasmic reticulum (ER) chaperone BiP (HSPA5) which is important for protein folding and quality control in the ER [ (PUBMED:26655470) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HSP70