Protein Domain : KilA, N-terminal/APSES-type HTH, DNA-binding IPR018004

Type	Domain
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 α-β fold with four conserved strands and at least two conserved helices []. Some proteins known to contain a KilA-N domain are listed below:Bacteriophage P1 protein kilA ( ). Fowlpox virus (FPV) protein FPV236 ( ). Trichomonas vaginalis G3 Putative uncharacterised protein ( ). Vaccinia virus hypothetical 21.7kDa HindIII-C protein ( ).
Short Name	KilA_N/APSES_HTH