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Comparative analysis data of SF1 and SF2 helicases from three domains of life
SF1 and SF2 helicases are important molecular motors that use the energy of ATP to unwind nucleic acids or nucleic-acid protein complexes. They are ubiquitous enzymes and found in almost all organisms sequenced to date. This article provides a comparative analysis for SF1 and SF2 helicase families f...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5349461/ https://www.ncbi.nlm.nih.gov/pubmed/28337468 http://dx.doi.org/10.1016/j.dib.2017.02.047 |
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author | Chaar, Wafi Ibrahim, Hiba Kozah, Juliana Chamieh, Hala |
author_facet | Chaar, Wafi Ibrahim, Hiba Kozah, Juliana Chamieh, Hala |
author_sort | Chaar, Wafi |
collection | PubMed |
description | SF1 and SF2 helicases are important molecular motors that use the energy of ATP to unwind nucleic acids or nucleic-acid protein complexes. They are ubiquitous enzymes and found in almost all organisms sequenced to date. This article provides a comparative analysis for SF1 and SF2 helicase families from three domains of life archaea, human, bacteria. Seven families are conserved in these three representatives and includes Upf1-like, UvrD-like, Rad3-like, DEAD-box, RecQ-like. Snf2 and Ski2-like. The data highlight conservation of the helicase core motifs for each of these families. Phylogenetic analysis presented on certain protein families are essential for further studies tracing the evolutionary history of helicase families. The data supplied in this article support publication “Genome-wide identification of SF1 and SF2 helicases from archaea” (Chamieh et al., 2016) [1]. |
format | Online Article Text |
id | pubmed-5349461 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-53494612017-03-23 Comparative analysis data of SF1 and SF2 helicases from three domains of life Chaar, Wafi Ibrahim, Hiba Kozah, Juliana Chamieh, Hala Data Brief Data Article SF1 and SF2 helicases are important molecular motors that use the energy of ATP to unwind nucleic acids or nucleic-acid protein complexes. They are ubiquitous enzymes and found in almost all organisms sequenced to date. This article provides a comparative analysis for SF1 and SF2 helicase families from three domains of life archaea, human, bacteria. Seven families are conserved in these three representatives and includes Upf1-like, UvrD-like, Rad3-like, DEAD-box, RecQ-like. Snf2 and Ski2-like. The data highlight conservation of the helicase core motifs for each of these families. Phylogenetic analysis presented on certain protein families are essential for further studies tracing the evolutionary history of helicase families. The data supplied in this article support publication “Genome-wide identification of SF1 and SF2 helicases from archaea” (Chamieh et al., 2016) [1]. Elsevier 2017-03-03 /pmc/articles/PMC5349461/ /pubmed/28337468 http://dx.doi.org/10.1016/j.dib.2017.02.047 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Data Article Chaar, Wafi Ibrahim, Hiba Kozah, Juliana Chamieh, Hala Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title | Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title_full | Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title_fullStr | Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title_full_unstemmed | Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title_short | Comparative analysis data of SF1 and SF2 helicases from three domains of life |
title_sort | comparative analysis data of sf1 and sf2 helicases from three domains of life |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5349461/ https://www.ncbi.nlm.nih.gov/pubmed/28337468 http://dx.doi.org/10.1016/j.dib.2017.02.047 |
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