AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl‐tRNA synthetases
The aminoacyl‐tRNA synthetases (aaRS) are a large group of enzymes that implement the genetic code in all known biological systems. They attach amino acids to their cognate tRNAs, moonlight in various translational and non‐translational activities beyond aminoacylation, and are linked to many geneti...
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| creator | Douglas, Jordan Cui, Haissi Perona, John J. Vargas‐Rodriguez, Oscar Tyynismaa, Henna Carreño, Claudia Alvarez Ling, Jiqiang Ribas de Pouplana, Lluís Yang, Xiang‐Lei Ibba, Michael Becker, Hubert Fischer, Frédéric Sissler, Marie Carter, Charles W. Wills, Peter R. |
| description | The aminoacyl‐tRNA synthetases (aaRS) are a large group of enzymes that implement the genetic code in all known biological systems. They attach amino acids to their cognate tRNAs, moonlight in various translational and non‐translational activities beyond aminoacylation, and are linked to many genetic disorders. The aaRS have a subtle ontology characterized by structural and functional idiosyncrasies that vary from organism to organism, and protein to protein. Across the tree of life, the 22 coded amino acids are handled by 16 evolutionary families of Class I aaRS and 21 families of Class II aaRS. We introduce AARS Online, an interactive Wikipedia‐like tool curated by an international consortium of field experts. This platform systematizes existing knowledge about the aaRS by showcasing a taxonomically diverse selection of aaRS sequences and structures. Through its graphical user interface, AARS Online facilitates a seamless exploration between protein sequence and structure, providing a friendly introduction to the material for non‐experts and a useful resource for experts. Curated multiple sequence alignments can be extracted for downstream analyses. Accessible at www.aars.online, AARS Online is a free resource to delve into the world of the aaRS. |
| doi_str_mv | 10.1002/iub.2911 |
| format | Article |
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Curated multiple sequence alignments can be extracted for downstream analyses. 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IUBMB Life published by Wiley Periodicals LLC on behalf of International Union of Biochemistry and Molecular Biology.</rights><rights>2024. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). 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They attach amino acids to their cognate tRNAs, moonlight in various translational and non‐translational activities beyond aminoacylation, and are linked to many genetic disorders. The aaRS have a subtle ontology characterized by structural and functional idiosyncrasies that vary from organism to organism, and protein to protein. Across the tree of life, the 22 coded amino acids are handled by 16 evolutionary families of Class I aaRS and 21 families of Class II aaRS. We introduce AARS Online, an interactive Wikipedia‐like tool curated by an international consortium of field experts. This platform systematizes existing knowledge about the aaRS by showcasing a taxonomically diverse selection of aaRS sequences and structures. Through its graphical user interface, AARS Online facilitates a seamless exploration between protein sequence and structure, providing a friendly introduction to the material for non‐experts and a useful resource for experts. 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| subjects | Amino Acid Sequence Amino acids Amino Acyl-tRNA Synthetases - chemistry Amino Acyl-tRNA Synthetases - genetics Amino Acyl-tRNA Synthetases - metabolism Aminoacylation aminoacyl‐tRNA synthetases Animals Databases, Protein Evolution, Molecular Genetic code Genetic disorders Humans Internet Life Sciences Protein structure Proteins Special Issue Structure-function relationships Transfer RNA Translation tRNA User-Computer Interface |
| title | AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl‐tRNA synthetases |
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