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97  structures 8991  species 0  interactions 92755  sequences 2024  architectures

Family: DnaJ (PF00226)

Summary: DnaJ domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

Chaperone DnaJ Edit Wikipedia article

DnaJ C terminal region

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-hydrolizing 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[1]. 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.

Besides stimulating the ATPase activity of DnaK through its J-domain, DnaJ also associates with unfolded polypeptide chains and prevents their aggregation[2]. 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.

This domain consists of the C-terminal region of the DnaJ protein. Although the function of this region is unknown, it is always found associated with InterPro: IPR001623 and InterPro: IPR001305.

Human proteins containing this domain



  1. ^ Douglas MG, Cyr DM, Langer T (1994). "DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70". Trends Biochem. Sci. 19 (4): 176–181. PMID 8016869.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ 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. PMID 15063739.
This article incorporates text from the public domain Pfam and InterPro: IPR002939

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


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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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.

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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: 62.5 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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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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
A0A044R4E4 View 3D Structure Click here
A0A044R4L9 View 3D Structure Click here
A0A044R6A8 View 3D Structure Click here
A0A044R6B3 View 3D Structure Click here
A0A044RAK8 View 3D Structure Click here
A0A044RRS4 View 3D Structure Click here
A0A044RYV3 View 3D Structure Click here
A0A044RZ41 View 3D Structure Click here
A0A044S5I5 View 3D Structure Click here
A0A044SNS8 View 3D Structure Click here
A0A044T3P6 View 3D Structure Click here
A0A044T7M6 View 3D Structure Click here
A0A044TBQ3 View 3D Structure Click here
A0A044TQC0 View 3D Structure Click here
A0A044TV98 View 3D Structure Click here
A0A044U440 View 3D Structure Click here
A0A044U458 View 3D Structure Click here
A0A044U464 View 3D Structure Click here
A0A044UIN8 View 3D Structure Click here
A0A044UMJ1 View 3D Structure Click here
A0A044V3T8 View 3D Structure Click here
A0A044V416 View 3D Structure Click here
A0A044V497 View 3D Structure Click here
A0A044V9A3 View 3D Structure Click here
A0A044VJ53 View 3D Structure Click here
A0A077YWD5 View 3D Structure Click here
A0A077YWP2 View 3D Structure Click here
A0A077YX04 View 3D Structure Click here
A0A077YZL7 View 3D Structure Click here
A0A077Z222 View 3D Structure Click here
A0A077Z2M6 View 3D Structure Click here
A0A077Z477 View 3D Structure Click here
A0A077Z6D3 View 3D Structure Click here
A0A077Z6L5 View 3D Structure Click here
A0A077Z798 View 3D Structure Click here
A0A077Z7B9 View 3D Structure Click here
A0A077Z819 View 3D Structure Click here
A0A077Z882 View 3D Structure Click here
A0A077ZAA4 View 3D Structure Click here
A0A077ZAR8 View 3D Structure Click here