The domain within your query sequence starts at position 1 and ends at position 154; the E-value for the ASF1_hist_chap domain shown below is 7.1e-75.
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSV LVGPVPAGRHMFVFQADAPNAGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTET ELRENPPVKPDFSKLQRNILASNPRVTRFHINWE
ASF1_hist_chap |
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PFAM accession number: | PF04729 |
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Interpro abstract (IPR006818): | This family includes the yeast and human ASF1 protein. These proteins have histone chaperone activity [ (PUBMED:14680630) ]. ASF1 participates in both the replication-dependent and replication-independent pathways. The structure three-dimensional has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers [ (PUBMED:10759893) ]. |
GO process: | chromatin assembly or disassembly (GO:0006333) |
GO component: | nucleus (GO:0005634) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ASF1_hist_chap