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97  structures 8991  species 0  interactions 92755  sequences 2024  architectures

Family: DnaJ (PF00226)

Summary: DnaJ domain

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This is the Wikipedia entry entitled "Chaperone DnaJ". More...

Chaperone DnaJ Edit Wikipedia article

DnaJ domain
PBB Protein DNAJB1 image.jpg
PDB rendering based on 1hdj.
DnaJ central domain
Pfam clanCL0518
DnaJ C terminal domain
PDB 1nlt EBI.jpg
the crystal structure of hsp40 ydj1

In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans.[1][2]


Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold.[3] DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.

This family of proteins contain a 70 amino acid consensus sequence known as the J domain. The J domain of DnaJ interacts with Hsp70 heat shock proteins.[4] DnaJ heat-shock proteins play a role in regulating the ATPase activity of Hsp70 heat-shock proteins.[5][6]

Besides stimulating the ATPase activity of DnaK through its J-domain, DnaJ also associates with unfolded polypeptide chains and prevents their aggregation.[7] Thus, DnaK and DnaJ may bind to one and the same polypeptide chain to form a ternary complex. The formation of a ternary complex may result in cis-interaction of the J-domain of DnaJ with the ATPase domain of DnaK. An unfolded polypeptide may enter the chaperone cycle by associating first either with ATP-liganded DnaK or with DnaJ. DnaK interacts with both the backbone and side chains of a peptide substrate; it thus shows binding polarity and admits only L-peptide segments. In contrast, DnaJ has been shown to bind both L- and D-peptides and is assumed to interact only with the side chains of the substrate.

Domain architecture

Proteins in this family consist of three domains. The N-terminal domain is the J domain (described above). The central domain is a cysteine-rich region, which 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. This domain has disulphide isomerase activity.[8] The function of the C-terminal is chaperone and dimerization.

Proteins containing a DnaJ domain


  1. ^ Qiu XB, Shao YM, Miao S, Wang L (November 2006). "The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones". Cellular and Molecular Life Sciences. 63 (22): 2560–70. doi:10.1007/s00018-006-6192-6. PMID 16952052.
  2. ^ Caplan AJ, Cyr DM, Douglas MG (June 1993). "Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins". Molecular Biology of the Cell. 4 (6): 555–63. doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
  3. ^ Douglas MG, Cyr DM, Langer T (1994). "DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70". Trends Biochem. Sci. 19 (4): 176–181. doi:10.1016/0968-0004(94)90281-x. PMID 8016869.
  4. ^ Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GL (July 2005). "Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions". Protein Science. 14 (7): 1697–709. doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
  5. ^ Fan CY, Lee S, Cyr DM (2003). "Mechanisms for regulation of Hsp70 function by Hsp40". Cell stress & chaperones. 8 (4): 309–16. doi:10.1379/1466-1268(2003)008<0309:MFROHF>2.0.CO;2. PMC 514902. PMID 15115283.
  6. ^ Ohtsuka K, Hata M (2000). "Molecular chaperone function of mammalian Hsp70 and Hsp40--a review". International Journal of Hyperthermia. 16 (3): 231–45. doi:10.1080/026567300285259. PMID 10830586.
  7. ^ Christen P, Han W (2004). "cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides". FEBS Lett. 563 (1): 146–150. doi:10.1016/S0014-5793(04)00290-X. PMID 15063739.
  8. ^ Martinez-Yamout, M.; Legge, G. B.; Zhang, O.; Wright, P. E.; Dyson, H. J. (2000). "Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ☆☆☆". Journal of Molecular Biology. 300 (4): 805–818. doi:10.1006/jmbi.2000.3923. PMID 10891270.
This article incorporates text from the public domain Pfam and InterPro: IPR002939
This article incorporates text from the public domain Pfam and InterPro: IPR001623
This article incorporates text from the public domain Pfam and InterPro: IPR001305

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

DnaJ domain Provide feedback

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].

Literature references

  1. Cyr DM, Langer T, Douglas MG; , Trends Biochem Sci 1994;19:176-181.: DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. PUBMED:8016869 EPMC:8016869

  2. Stubdal H, Zalvide J, Campbell KS, Schweitzer C, Roberts TM, DeCaprio JA; , Mol Cell Biol 1997;17:4979-4990.: Inactivation of pRB-related proteins p130 and p107 mediated by the J domain of simian virus 40 large T antigen. PUBMED:9271376 EPMC:9271376

  3. Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wuthrich K; , J Mol Biol 1996;260:236-250.: NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. PUBMED:8764403 EPMC:8764403

  4. Kelley WL; , Trends Biochem Sci 1998;23:222-227.: The J-domain family and the recruitment of chaperone power. PUBMED:9644977 EPMC:9644977

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001623

The hsp70 chaperone machine performs many diverse roles in the cell, including folding of nascent proteins, translocation of polypeptides across organelle membranes, coordinating responses to stress, and targeting selected proteins for degradation. DnaJ is a member of the hsp40 family of molecular chaperones, which is also called the J-protein family, the members of which regulate the activity of hsp70s. DnaJ (hsp40) binds to dnaK (hsp70) and stimulates its ATPase activity, generating the ADP-bound state of dnaK, which interacts stably with the polypeptide substrate [ PUBMED:11395418 , PUBMED:15170475 ].

Structurally, the DnaJ protein consists of an N-terminal conserved domain (called 'J' domain) of about 70 amino acids, a glycine-rich region ('G' domain') of about 30 residues, a central domain containing four repeats of a CXXCXGXG motif ('CRR' domain) and a C-terminal region of 120 to 170 residues.

Such a structure is shown in the following schematic representation:

  | J-domain   | | Gly-R |     | CXXCXGXG  | C-terminal                     |

The structure of the J-domain has been solved [ PUBMED:8764403 ]. The J domain consists of four helices, the second of which has a charged surface that includes basic residues that are essential for interaction with the ATPase domain of hsp70 [ PUBMED:12454054 ].

J-domains are found in many prokaryotic and eukaryotic proteins [ PUBMED:1585456 ]. In yeast, three J-like proteins have been identified containing regions closely resembling a J-domain, but lacking the conserved HPD motif - these proteins do not appear to act as molecular chaperones [ PUBMED:15170475 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Chaperone-J (CL0392), which has the following description:

The J-domain is found in a number of stress-response proteins. It is found at the N-terminal of Hsc20, DnaJ-chaperone in E. coli, and viral large T-antigen proteins; it is also in Hsc40, mammalian auxilin and in both animal and plant DnaJ proteins. It is also found in degenerate form in Pam16 proteins.

The clan contains the following 2 members:

DnaJ Pam16


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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Birney E , Finn RD
Number in seed: 222
Number in full: 92755
Average length of the domain: 62.50 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 15.03 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.8 27.8
Trusted cut-off 27.8 27.8
Noise cut-off 27.7 27.7
Model length: 63
Family (HMM) version: 34
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DnaJ domain has been found. There are 97 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096TC93 View 3D Structure Click here
A0A0G2JTM9 View 3D Structure Click here
A0A0G2JTP0 View 3D Structure Click here
A0A0G2JUJ9 View 3D Structure Click here
A0A0G2JYE9 View 3D Structure Click here
A0A0G2K435 View 3D Structure Click here
A0A0G2K5E4 View 3D Structure Click here
A0A0G2K9H9 View 3D Structure Click here
A0A0G2QC19 View 3D Structure Click here
A0A0N7KLP7 View 3D Structure Click here
A0A0P0UXD4 View 3D Structure Click here
A0A0P0V788 View 3D Structure Click here
A0A0P0VG31 View 3D Structure Click here
A0A0P0VPW3 View 3D Structure Click here
A0A0P0VVB5 View 3D Structure Click here
A0A0P0WLE7 View 3D Structure Click here
A0A0P0WLJ5 View 3D Structure Click here
A0A0P0WM26 View 3D Structure Click here
A0A0P0WQ21 View 3D Structure Click here
A0A0P0WWX5 View 3D Structure Click here
A0A0P0XM04 View 3D Structure Click here
A0A0P0XYL0 View 3D Structure Click here
A0A0P0Y0Q1 View 3D Structure Click here
A0A0P0Y3F3 View 3D Structure Click here
A0A0P0Y3S7 View 3D Structure Click here
A0A0P0YD84 View 3D Structure Click here
A0A0R0E480 View 3D Structure Click here
A0A0R0E5N2 View 3D Structure Click here
A0A0R0EK66 View 3D Structure Click here
A0A0R0EL68 View 3D Structure Click here
A0A0R0EVG5 View 3D Structure Click here
A0A0R0FDV7 View 3D Structure Click here
A0A0R0FIR6 View 3D Structure Click here
A0A0R0GKU5 View 3D Structure Click here
A0A0R0GQY1 View 3D Structure Click here
A0A0R0I0F5 View 3D Structure Click here
A0A0R0I1S1 View 3D Structure Click here
A0A0R0I6W3 View 3D Structure Click here
A0A0R0ILH6 View 3D Structure Click here
A0A0R0IQC6 View 3D Structure Click here