Protein sequence comparisons show that the pseudoproteases encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family

Amino acid sequence comparisons show extensive similarities among the deoxyuridine triphosphatases (dUTPases) of Escherichia coli and of herpesviruses, and the 'protease-like' or 'pseudoprotease' sequences encoded by certain retroviruses in the oncovirus and lentivirus families a...

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Bibliographic Details
Published in:Nucleic acids research 1990-07, Vol.18 (14), p.4105-4110
Main Author: MCGEOCH, D. J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genes. Genome
Herpesviridae - enzymology
Herpesviridae - genetics
Herpesvirus
Lentivirus
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Multigene Family
Peptide Hydrolases - genetics
Poxviridae - enzymology
Poxviridae - genetics
Pyrophosphatases - genetics
Retroviridae - enzymology
Retroviridae - genetics
Retrovirus
Sequence Homology, Nucleic Acid
Sugar Phosphates - metabolism
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Summary:Amino acid sequence comparisons show extensive similarities among the deoxyuridine triphosphatases (dUTPases) of Escherichia coli and of herpesviruses, and the 'protease-like' or 'pseudoprotease' sequences encoded by certain retroviruses in the oncovirus and lentivirus families and by poxviruses. These relationships suggest strongly that the 'pseudoproteases' actually are dUTPases, and have not arisen by duplication of an oncovirus protease gene as had been suggested. The herpesvirus dUTPase sequences differ from the others in that they are longer (about 370 residues, against around 140) and one conserved element ('Motif 3') is displaced relative to its position in the other sequences; a model involving internal duplication of the herpesvirus gene can account effectively for these observations. Sequences closely similar to Motif 3 are also found in phosphofructokinases, where they form part of the active site and fructose phosphate binding structure; thus these sequences may represent a class of structural element generally involved in phosphate transfer to and from glycosides.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/18.14.4105