In molecular biology, the HD domain is a conserved protein domain, named after the conserved histidine (H) and/or aspartate (D) amino acid residues. It is found in a superfamily of enzymes with a predicted or known phosphohydrolase activity. These enzymes appear to be involved in nucleic acid metabolism, signal transduction and possibly other functions in bacteria, archaea and eukaryotes. The fact that all the highly conserved residues in the HD superfamily are histidines or aspartates suggests that coordination of divalent cations is essential for the activity of these proteins.[1]

HD domain
crystal structure of o67745, a hypothetical protein from aquifex aeolicus at 2.0 a resolution.
Identifiers
SymbolHD
PfamPF01966
Pfam clanCL0237
InterProIPR006674
PROSITEPDOC00924
SCOP21f62 / SCOPe / SUPFAM
CDDcd00077
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

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  1. ^ Aravind L, Koonin EV (December 1998). "The HD domain defines a new superfamily of metal-dependent phosphohydrolases". Trends in Biochemical Sciences. 23 (12): 469–72. doi:10.1016/s0968-0004(98)01293-6. PMID 9868367.
This article incorporates text from the public domain Pfam and InterPro: IPR006674