ribbon-helix-helix domain of CopG family transcriptional regulators found in archaea
This subfamily includes the N-terminal ribbon-helix-helix (RHH) domain of putative transcriptional repressor CopG from archaea, and similar proteins. These uncharacterized proteins have a typical RHH, similar to plasmid-encoded transcriptional repressor CopG, the protein that is encoded by the promiscuous streptococcal plasmid pMV158 and is involved in the control of plasmid copy number.
Comment:based on dimeric structures of other family members
Comment:The ribbon-helix-helix (RHH) type DNA-binding motif of the antitoxin is arranged as two antiparallel beta-strands which compose a ribbon, with each strand coming from one of two protein monomers; the beta-strands are involved both in dimer formation and in specific interactions with the DNA by fitting snugly into the major groove
Jiyao W et al.(2023). "The conserved domain database in 2023.",