Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins
The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to methylated lysine 4 of histone H3 (H3K4me), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling.
Conserved feature residue pattern:C C H C C C C C H C C H
Evidence:
Comment:based on the structure evidence that human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6 (PDB 4NN2) binds three Zn2+ ions through its ePHD finger
Comment:The extended PHD finger is characterized by Cys2HisCys5HisCys2His.
Jiyao W et al.(2023). "The conserved domain database in 2023.",