 CHZHistone chaperone domain CHZ | |
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| SMART ACC: | SM001082 |
| Description: | This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones (PUBMED:17289584). |
| InterPro ACC: | IPR019098 |
| InterPro abstract: | This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones [ expand |
| Family alignment: | View the Family alignment or the Alignment consensus sequence |
| There are 1 023 CHZ domains in 981 proteins in SMART's NRDB database. | |
Taxonomic distribution of proteins containing CHZ domains
The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing CHZ domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.
Predicted cellular role
| Cellular role: | Interaction (with the environment) |
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Relevant references for this domain
Primary literature for the CHZ domain is listed below. Automatically-derived, secondary literature is also available.
KEGG pathways involving proteins which contain this domain
This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a CHZ domain which could be assigned to a KEGG orthologous group, and not all proteins containing CHZ domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.