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.[1] Its name reflects some of the proteins that contain it: NAIP (NLP family apoptosis inhibitor protein), CIITA (that is, C2TA or MHC class II transcription activator), HET-E (incompatibility locus protein from Podospora anserina) and TEP1 (that is, TP1 or telomerase-associated protein).

NACHT ___domain
Identifiers
SymbolNACHT
PfamPF05729
InterProIPR007111
PROSITEPS50837
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The NACHT ___domain contains 300 to 400 amino acids. It is a predicted nucleoside-triphosphatase (NTPase) ___domain, which is found in animal, fungal and bacterial proteins. It is found in association with other domains, such as the caspase recruitment ___domain (InterProIPR001315), the pyrin ___domain (InterProIPR004020), the HEAT repeat ___domain (InterProIPR004155), the WD40 repeat (InterProIPR001680), the leucine-rich repeat (LRR) or the BIR repeat (InterProIPR001370).[1]

The NACHT ___domain consists of seven distinct conserved motifs, including the ATP/GTPase specific P-loop, the Mg2+-binding site (Walker A and B motifs, respectively) and five more specific motifs. The unique features of the NACHT ___domain include the prevalence of 'tiny' residues (glycine, alanine or serine) 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.[1]

Examples

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Human proteins containing this ___domain include:

References

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  1. ^ a b c Koonin EV, Aravind L (May 2000). "The NACHT family - a new group of predicted NTPases implicated in apoptosis and MHC transcription activation". Trends in Biochemical Sciences. 25 (5): 223–4. doi:10.1016/S0968-0004(00)01577-2. PMID 10782090.
This article incorporates text from the public ___domain Pfam and InterPro: IPR007111