NACHT domain


The NACHT domain is an evolutionarily conserved protein domain. This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription. Its name reflects some of the proteins that contain it: NAIP, CIITA, HET-E and TEP1.
The NACHT domain contains 300 to 400 amino acids. It is a predicted nucleoside-triphosphatase domain, which is found in animal, fungal and bacterial proteins. It is found in association with other domains, such as the CARD domain, the pyrin domain, the HEAT repeat domain, the WD40 repeat, the leucine-rich repeat or the BIR repeat.
The NACHT domain consists of seven distinct conserved motifs, including the ATP/GTPase specific P-loop, the Mg2+-binding site and five more specific motifs. The unique features of the NACHT domain include the prevalence of 'tiny' residues directly C-terminal of the Mg2+-coordinating aspartate in the Walker B motif, in place of a second acidic residue prevalent in other NTPases. A second acidic residue is typically found in the NACHT-containing proteins two positions downstream. Furthermore, the distal motif VII contains a conserved pattern of polar, aromatic and hydrophobic residues that is not seen in any other NTPase family.

Examples

Human proteins containing this domain include: