2019
DOI: 10.1007/s00705-019-04292-z
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Characterization of the endonuclease activity of the replication-associated protein of beak and feather disease virus

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Cited by 5 publications
(2 citation statements)
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“…We identified 13 putative Reps in these crucivirus genomes that lack all four motifs typically found in S3H helicases (e.g., CruV-166, CruV-202, and CruV-499 [ Table S4]). Recent work has shown that the deletion of individual conserved motifs in the helicase domain of the Rep protein of beak and feather disease virus does not abolish ATPase and GTPase activity (66). The absence of all four motifs may prevent these putative Reps from performing helicase and ATPase activity using previously characterized mechanisms.…”
Section: Resultsmentioning
confidence: 99%
“…We identified 13 putative Reps in these crucivirus genomes that lack all four motifs typically found in S3H helicases (e.g., CruV-166, CruV-202, and CruV-499 [ Table S4]). Recent work has shown that the deletion of individual conserved motifs in the helicase domain of the Rep protein of beak and feather disease virus does not abolish ATPase and GTPase activity (66). The absence of all four motifs may prevent these putative Reps from performing helicase and ATPase activity using previously characterized mechanisms.…”
Section: Resultsmentioning
confidence: 99%
“…Table 4). Recent work has shown that the deletion of individual conserved motifs in the helicase domain of the Rep protein of beak and feather disease virus does not abolish ATPase and GTPase activity (86). The absence of all four motifs may prevent these putative Reps from performing helicase and ATPase activity using previously characterized mechanisms.…”
Section: Crucivirus Repmentioning
confidence: 99%