PMID:8771213

Citation	Koonin, EV and Rudd, KE (1996) Two domains of superfamily I helicases may exist as separate proteins. Protein Sci. 5:178-80
Abstract	DNA and RNA helicases of superfamily I are characterized by seven conserved motifs. The five N-terminal motifs are separated from the two C-terminal ones by a spacer that is highly variable in both sequence and length, suggesting the existence of two distinct domains. Using computer methods for protein sequence analysis, we show that PhoH, an ATP-binding protein that is conserved in Escherichia coli and Mycobacterium leprae, is homologous to the putative N-terminal domain of the helicases, whereas the putative E. coli protein YjhR is homologous to the C-terminal domain. These findings suggest that the N-and C-terminal domains of superfamily I helicases have distinct activities, with only the N-terminal domain having the ATPase activity. It is speculated that PhoH and YjhR have evolved from helicases through deletion of the portions of the helicase genes coding for the C- and N-terminal domain, respectively.
Links	PubMed PMC2143243 Online version:10.1002/pro.5560050124
Keywords	Amino Acid Sequence; Conserved Sequence; DNA Helicases/chemistry; Escherichia coli/chemistry; Molecular Sequence Data; Mycobacterium leprae/chemistry; RNA Helicases; RNA Nucleotidyltransferases/chemistry; Sequence Homology, Amino Acid
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