Protein Family Models

DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature [2]. [1]. 8016869. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Cyr DM, Langer T, Douglas MG;. Trends Biochem Sci 1994;19:176-181. [2]. 9271376. Inactivation of pRB-related proteins p130 and p107 mediated by the J domain of simian virus 40 large T antigen. Stubdal H, Zalvide J, Campbell KS, Schweitzer C, Roberts TM, DeCaprio JA;. Mol Cell Biol 1997;17:4979-4990. The structure of the DnaJ domain by NMR. [3]. 8764403. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wuthrich K;. J Mol Biol 1996;260:236-250. [4]. 9644977. The J-domain family and the recruitment of chaperone power. Kelley WL;. Trends Biochem Sci 1998;23:222-227. (from Pfam)

Date:

2024-10-16

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

Date:

2024-05-28