The domain within your query sequence starts at position 404 and ends at position 507; the E-value for the CENP-T_C domain shown below is 5.4e-36.



PFAM accession number:PF15511
Interpro abstract (IPR035425):

This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin [(PUBMED:21464230), (PUBMED:22304917)]. Proteins containing this domain also include Histone H4.

CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes [(PUBMED:22391098), (PUBMED:21464230), (PUBMED:22304917)].

Histone H4 is one of the five histones, along with H1/H5, H2A, H2B and H3. Two copies of each of the H2A, H2B, H3, and H4 histones ensemble to form the core of the nucleosome [(PUBMED:16472024)]. The nucleosome forms octameric structure that wraps DNA in a left-handed manner. H3 is a highly conserved protein of 135 amino acid residues [(PUBMED:8121801), (PUBMED:2041803)]. Histones can undergo several different types of post-translational modifications that affect transcription, DNA repair, DNA replication and chromosomal stability. The sequence of histone H4 has remained almost invariant in more then 2 billion years of evolution [(PUBMED:8121801), (PUBMED:6808351), (PUBMED:3340182)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CENP-T_C