Multiple sequence alignment of ARID in ARID-BAF250_C architecture (ARCH2).

The regions marked in yellow show the ARID-specific conserved signature sequence that is seen in all ARIDs across various domain architectures. Residue positions highlighted in red indicate signature residues in ARID that were selectively conserved in combination with BAF250_C. The derived biochemical property-based ARID consensus sequence for ARCH2 at 70% conservation threshold is shown below the alignment using the associated MView symbol as follows: uppercase–standard amino acid notation; alcohol(o)—S,T; aliphatic (l)—I,L,V; aromatic(a)–F,H,W,Y; charged(c)–D,E,H,K,R; hydrophobic(h)—A,C,F,G,H,I,K,L,M,R,T,V,W,Y; negative(-)—D,E polar(p)—C, D,E,H,K,N,Q,R,S,T; positive(+)—H,K,R; small(s)—A,C,D,G,N,P,S,T,V; tiny(u)—A,G,S; turn like(t)—A,C,D,E,G,H,K,N,Q,R,S,T. Secondary structure of ARCH2 representative BAF250a ARID (PDB ID: 1RYU), in a red rectangular box in the alignments) is shown at the bottom of the alignment as well. Previously reported DNA binding residues in 1RYU are marked with black box. The biochemical property-based uniquely conserved residue positions of ARCH2 in the consensus sequence are marked with (*).