The amino-terminal module of the poxvirus D6R/NIR proteins defines a novel conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses [ PUBMED:11897024 ]. Putative proteins with homology to the KilA-N domain have also been identified in Maverick … expand

The amino-terminal module of the poxvirus D6R/NIR proteins defines a novel conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses [ PUBMED:11897024 ]. Putative proteins with homology to the KilA-N domain have also been identified in Maverick transposable elements of the parabasalid protozoa Trichomonas vaginalis [ PUBMED:17034960 ]. The KilA-N domain has been suggested to be homologous to the fungal DNA-binding APSES domain. In all proteins shown to contain the KilA-N domain, it occurs at the extreme amino terminus accompanied by a wide range of distinct carboxy-terminal domains. These carboxy-terminal modules may be enzymes, such as the nuclease domains, or might mediate additional, specific interactions with nucleic acids or proteins, like the RING or CCCH fingers in the poxviruses [ PUBMED:11897024 ]. The KilA-N domain is predicted to adopt an α-β fold with four conserved strands and at least two conserved helices [ PUBMED:11897024 ]. Some proteins known to contain a KilA-N domain are listed below:

• Cell pattern formation-associated protein stuA ( Q4X228 ).
• Host range factor p28 ( Q76R05 ).
• Bacteriophage P1 protein kilA ( P19653 ).
• Fowlpox virus (FPV) protein FPV236 ( P14365 ).