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

curved DNA-binding protein is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock

Date:

2019-08-20

Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock

Gene:

cbpA

Date:

2021-11-04