FDX-ACBFerredoxin-fold anticodon binding domain
|SMART accession number:||SM00896|
|Description:||This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).|
|Interpro abstract (IPR005121):|
Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to their cognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among the most complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it [(PUBMED:7664121), (PUBMED:9016717), (PUBMED:10049785), (PUBMED:12962494), (PUBMED:18611382)].
|GO process:||tRNA processing (GO:0008033), phenylalanyl-tRNA aminoacylation (GO:0006432)|
|GO function:||phenylalanine-tRNA ligase activity (GO:0004826), magnesium ion binding (GO:0000287), tRNA binding (GO:0000049), ATP binding (GO:0005524)|
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