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The annotation and conditions in this rule are derived from the following entries: P08622 (DNAJ_ECOLI)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 147 - 147 aligns to "C" in entry P08622 Subsequence at position 200 - 200 aligns to "C" in entry P08622 Subsequence at position 144 - 144 aligns to "C" in entry P08622 Subsequence at position 197 - 197 aligns to "C" in entry P08622
    • Subsequence at position 164 - 164 aligns to "C" in entry P08622 Subsequence at position 183 - 183 aligns to "C" in entry P08622 Subsequence at position 161 - 161 aligns to "C" in entry P08622 Subsequence at position 186 - 186 aligns to "C" in entry P08622
  • Subsequence at position 147 - 147 aligns to "C" in entry P08622 (applies "Zinc 1") Subsequence at position 200 - 200 aligns to "C" in entry P08622 (applies "Zinc 1") Subsequence at position 144 - 144 aligns to "C" in entry P08622 (applies "Zinc 1") Subsequence at position 197 - 197 aligns to "C" in entry P08622 (applies "Zinc 1")
  • Subsequence at position 164 - 164 aligns to "C" in entry P08622 (applies "Zinc 2") Subsequence at position 183 - 183 aligns to "C" in entry P08622 (applies "Zinc 2") Subsequence at position 161 - 161 aligns to "C" in entry P08622 (applies "Zinc 2") Subsequence at position 186 - 186 aligns to "C" in entry P08622 (applies "Zinc 2")
  • Subsequence at position 144 - 151 aligns to "C-x(2)-C-x-G-x-G" in entry P08622 (applies "CXXCXGXG motif") Subsequence at position 161 - 168 aligns to "C-x(2)-C-x-G-x-G" in entry P08622 (applies "CXXCXGXG motif") Subsequence at position 197 - 204 aligns to "C-x(2)-C-x-G-x-G" in entry P08622 (applies "CXXCXGXG motif") Subsequence at position 183 - 190 aligns to "C-x(2)-C-x-G-x-G" in entry P08622 (applies "CXXCXGXG motif")
    • Subsequence at position 77 - 114 aligns to entry P08622

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    Chaperone protein DnaJ

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namei

  • Name:dnaJ

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

  • The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • 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. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homodimer.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Zinc 1 (to residues corresponding to position 147)
  • Zinc 1 (to residues corresponding to position 200)
  • Zinc 1 (to residues corresponding to position 144)
  • Zinc 1 (to residues corresponding to position 197)
  • Zinc 2 (to residues corresponding to position 164)
  • Zinc 2 (to residues corresponding to position 183)
  • Zinc 2 (to residues corresponding to position 161)
  • Zinc 2 (to residues corresponding to position 186)

<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi

  • Gly-rich (to residues corresponding to positions 77 - 114)

<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati

  • CXXCXGXG motif (to residues corresponding to positions 144 - 151)
  • CXXCXGXG motif (to residues corresponding to positions 161 - 168)
  • CXXCXGXG motif (to residues corresponding to positions 197 - 204)
  • CXXCXGXG motif (to residues corresponding to positions 183 - 190)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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