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Phosphohydrolase-associated domain
This domain is found on bacterial and archaeal metal-dependent phosphohydrolases. (from Pfam)
HD domain-containing protein
HD domains are metal dependent phosphohydrolases. [1]. 9868367. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:469-472. (from Pfam)
deoxyguanosinetriphosphate triphosphohydrolase family protein
deoxyguanosinetriphosphate triphosphohydrolase family protein similar to deoxyguanosinetriphosphate (dGTP) triphosphohydrolase, which catalyzes the hydrolysis of dGTP to form deoxyguanosine and triphosphate
deoxyguanosinetriphosphate triphosphohydrolase
dGTP triphosphohydrolase
dGTP triphosphohydrolase (dgt) releases inorganic triphosphate, an unusual activity reaction product, from GTP. Its activity has been called limited to the Enterobacteriaceae, although homologous sequences are detected elsewhere. This finding casts doubt on whether the activity is shared in other species. In several of these other species, the homologous gene is found in an apparent operon with dnaG, the DNA primase gene. The enzyme from E. coli was shown to bind coopertatively to single stranded DNA. The biological role of dgt is unknown.
HDIG domain-containing metalloprotein
This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. For proteins scoring above the trusted cutoff, confidence is high both that the domain is present and that the HMM produces an essentially correct alignment. Protein regions scoring between the trusted and noise cutoffs include correctly aligned domains, homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits indications of homology.
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