Conserved Protein Domain Family
PHP

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cl23724: PHP Superfamily 
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Polymerase and Histidinol Phosphatase domain
The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Links
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Taxonomy: root
PubMed: 12 links
Protein: Related Protein
Related Structure
Statistics
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Accession: cl23724
PSSM Id: 451507
Name: PHP
Created: 2-Feb-2016
Updated: 8-Mar-2022
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