| URL: | http://rose.man.poznan.pl/aars/index |
| Full name: | The aminoacyl-tRNA synthetases |
| Description: | The aminoacyl-tRNA synthetases (AARS) are a diverse group of enzymes that ensure the fidelity of transfer of genetic information from DNA into protein. They catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. |
| Year founded: | 1999 |
| Last update: | 2000 |
| Version: | |
| Accessibility: |
Unaccessible
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| Country/Region: | Poland |
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| University/Institution: | Institute of Bioorganic Chemistry of the Polish Academy of Sciences |
| Address: | Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznan, Poland |
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| Province/State: | |
| Country/Region: | Poland |
| Contact name (PI/Team): | Jan Barciszewskia |
| Contact email (PI/Helpdesk): | jbarcisz@ibch.poznan.pl |
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Aminoacyl-tRNA synthetases database Y2K. [PMID: 10592262]
The aminoacyl-tRNA synthetases (AARS) are a diverse group of enzymes that ensure the fidelity of transfer of genetic information from DNA into protein. They catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. Currently, 818 AARS primary structures have been reported from archaebacteria, eubacteria, mitochondria, chloro-plasts and eukaryotic cells. The database is a compilation of the amino acid sequences of all AARSs, known to date, which are available as separate entries or alignments of related proteins via the WWW at http://rose.man.poznan.pl/aars/index.html |
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The aminoacyl-tRNA Synthetase Data Bank (AARSDB). [PMID: 9847219]
Aminoacyl-tRNA synthetases (AARSs) are the key components of the protein biosynthesis machinery. They are responsible for maintaining the fidelity of transfer of genetic information from DNA into protein. The database is a compilation of amino acid sequences of all aminoacyl-tRNA synthetases known to date. It contains 422 primary structures of the AARSs available as separate entries or alignments of related proteins. The database is available via the World Wide Web at http://rose.man.poznan.pl/aars/index.html |