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Hsp70 family protein
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. [1]. 9476895. The Hsp70 and Hsp60 chaperone machines. Bukau B, Horwich AL;. Cell 1998;92:351-366. (from Pfam)
Hsp70 (heat shock protein 70) family protein is a molecular chaperone involved in DNA replication, protein folding and the stress response; similar to Grapevine leafroll-associated virus movement protein Hsp70h, which transports viral genomes to neighboring plant cells directly through the plasmodesmata
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