Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins
ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Feature 1:putative peptide binding site [polypeptide binding site]
Evidence:
Comment:based on the structures of other Tudor domain superfamily members with bound methylated/dimethylated peptides
Comment:In general, the Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Jiyao W et al.(2023). "The conserved domain database in 2023.",