Prediction of terminal protein and ribonuclease H domains in the gene P product of hepadnaviruses.
By means of comparative analysis of primary and secondary structures, and hydropathy plots of hepadnavirus P proteins new functional domains were revealed additionally to the polymerase domain which had been found earlier in these proteins. The C-terminal part of P proteins was revealed to be significantly similar to ribonuclease H of E. coli. The ribonuclease H functional domain is known to be an integral entity of retrovirus reverse transcriptase as a rule. Availability of this domain indicates once more the putative reverse transcriptase properties of the P products. The proteins of hepadnaviruses were compared to terminal proteins of picornaviruses, adenoviruses and bacteriophages. The data obtained suggested that a conservative N-terminal region of P proteins functions as protein primer for DNA synthesis in hepadnaviruses.
Khudyakov YuE
D.I. Ivanovsky Institute of Virology, Academy of Medical Sciences, Moscow, USSR.
Makhov
A M
AM
D000595:Amino Acid Sequence; D004259:DNA-Directed DNA Polymerase; D004722:Endoribonucleases; D004926:Escherichia coli / Q000201:enzymology; D005814:Genes, Viral; D006518:Hepatitis Viruses / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012194:RNA-Directed DNA Polymerase; D016914:Ribonuclease H; D014764:Viral Proteins / Q000235:genetics
D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H