| Type: | Domain | Name: | KilA, N-terminal/APSES-type HTH, DNA-binding |
| Description: | 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 []. Putative proteins with homology to the KilA-N domain have also been identified in Maverick transposable elements of the parabasalid protozoa Trichomonas vaginalis[]. The KilA-N domain has been suggested to be homologous to the fungal DNA-binding APSES domain (see ). 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 (see ) or CCCH fingers in the poxviruses []. The KilA-N domain is predicted to adopt an alpha-beta fold with four conserved strands and at least two conserved helices []. Some proteins known to contain a KilA-N domain are listed below:Bacteriophage P1protein kilA ().Fowlpox virus(FPV) protein FPV236 (). Trichomonas vaginalis G3Putative uncharacterised protein ().Vaccinia virushypothetical 21.7 kDa HindIII-C protein (). | Short Name: | KilA_N/APSES_HTH |
