Protein Family Models

This family consists of the C terminal region of the DnaJ protein. It is always found associated with Pfam:PF00226 and Pfam:PF00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions [2]. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region [3]. [1]. 9644977. The J-domain family and the recruitment of chaperone power. Kelley WL;. Trends Biochem Sci 1998;23:222-227. [2]. 22011374. Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1. Silva JC, Borges JC, Cyr DM, Ramos CH, Torriani IL;. BMC Struct Biol. 2011;11:40. [3]. 14656432. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Li J, Qian X, Sha B;. Structure. 2003;11:1475-1483. (from Pfam)

Date:

2024-10-16

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

The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found [1]. [1]. 10891270. Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ. Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ;. J Mol Biol 2000;300:805-818. [2]. 14656432. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Li J, Qian X, Sha B;. Structure. 2003;11:1475-1483. (from Pfam)

Date:

2024-10-16

molecular chaperone DnaJ, part of the DnaK-DnaJ-GrpE system, prevents the aggregation of unfolded substrate and acts primarily by stimulating the ATPase activity of Hsp70

Date:

2024-12-06

This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.

Gene:

dnaJ

Date:

2024-05-30

Chaperone Hsp40; co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, dnaK-independent fashion

Gene:

dnaJ

Date:

2020-10-26