Summary
DnaJ domain
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
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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
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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
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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
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Kelley WL; , Trends Biochem Sci 1998;23:222-227.: The J-domain family and the recruitment of chaperone power. PUBMED:9644977
InterPro entry IPR001623
The prokaryotic heat shock protein DnaJ interacts with the chaperone hsp70-like DnaK protein PUBMED:8016869. 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:
+------------+-+-------+-----+-----------+--------------------------------+ | N-terminal | | Gly-R | | CXXCXGXG | C-terminal | +------------+-+-------+-----+-----------+--------------------------------+
It is thought that the 'J' domain of DnaJ mediates the interaction with the dnaK protein and consists of four helices, the second of which has a charged surface that includes at least one pair of basic residues that are essential for interaction with the ATPase domain of Hsp70. The J- and CRR-domains are found in many prokaryotic and eukaryotic proteins PUBMED:1585456, either together or separately. In yeast, J-domains have been classified into 3 groups; the class III proteins are functionally distinct and do not appear to act as molecular chaperones PUBMED:15170475.
Clan
This family is a member of clan Chaperone-J (CL0392), which contains the following 2 members:
DnaJ Pam16Gene Ontology
| Molecular function | heat shock protein binding (GO:0031072) |
External database links
| HOMSTRAD: | DnaJ |
| PANDIT: | PF00226 |
| PRINTS: | PR00625 |
| PROSITE: | PDOC00553 |
| SCOP: | 1xbl |
| SYSTERS: | DnaJ |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
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...
Trees
This page displays the phylogenetic tree for this family. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Birney E, Finn RD |
| Number in seed: | 258 |
| Number in full: | 11917 |
| Average length of the domain: | 62.10 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 16.82 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 64 | ||||||||||||
| Family (HMM) version: | 24 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Structures
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.
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