Phenylalanyl-tRNA synthetases [L-phenylalanine:tRNAPhe ligase (AMP-forming), EC 6.1.1.20] from Escherichia coli, yeast cytoplasm, and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl-tRNA synthetase. Both subunits are required for activity. We show here that a single mitochondrial polypeptide from Saccharomyces cerevisiae is an active phenylalanyl-tRNA synthetase. This protein (the MSF1 gene product) is active as a monomer. It has all three characteristic sequence motifs of the class II aminoacyl-tRNA synthetases, and its activity may result from the recruitment of additional sequences into an alpha-subunit-like structure.
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| Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
|---|---|---|---|---|---|---|
| Phenylalanyl-tRNA synthetase complex | involved in | phenylalanyl-tRNA aminoacylation | IDA | ComplexPortal | 2020-09-10 | |
| Phenylalanyl-tRNA synthetase complex | enables | ATP binding | IDA | ComplexPortal | 2020-09-10 | |
| Phenylalanyl-tRNA synthetase complex | enables | tRNA binding | IPI | ComplexPortal | 2020-09-10 | |
| Phenylalanyl-tRNA synthetase complex | enables | phenylalanine-tRNA ligase activity | IDA | ComplexPortal | 2020-09-10 |