kromodomainit
Kromodomain proteins are a family of chromatin-associated factors characterized by the presence of a conserved Kromodomain (KD), a structural motif typically found in proteins that interact with histones. These domains are named after the first identified member, the Drosophila HP1 protein, which was later renamed as Heterochromatin Protein 1 (HP1). The Kromodomain is approximately 50–60 amino acids long and is often found in proteins involved in transcriptional regulation, chromatin remodeling, and epigenetic inheritance.
The Kromodomain is structurally similar to the chromodomain, another histone-binding module, but differs in its sequence
Kromodomain-containing proteins play critical roles in maintaining cellular identity by reinforcing transcriptional silencing. For example, HP1
Structurally, the Kromodomain adopts a compact fold consisting of a five-stranded β-sheet and two α-helices, forming