v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | This entry represents a PHP-like (Polymerase and Histidinol Phosphatase) domain, the catalytic site of which has four motifs with conserved histidine residues. This domain has a 7-stranded β/α barrel fold; this structure shows some similarity to the TIM-barrel fold metallohydrolases. PHP-like domains are found in alpha-subunit of bacterial DNA polymerase III ( ) and family X DNA polymerases in addition to histidinol phosphatase ( ) [ ]. Proteins carrying a distorted (α/β)7 barrel PHP-like fold include the hypothetical protein YcdX from Escherichia coli (which contains a trinuclear metal-binding site on the C-terminal side of the barrel) [, ], as well as ribonuclease P protein component 3 (Rnp3) () from Pyrococcus horikoshii (no metal site on the C-terminal side of the barrel) [ ]. |
Short Name | Pol/histidinol_Pase-like |