| Accession | TIGR00469 |
| Name | pheS_mito |
| Function | phenylalanine--tRNA ligase |
| Gene Symbol | pheS |
| Trusted Cutoff | 258.35 |
| Domain Trusted Cutoff | 258.35 |
| Noise Cutoff | 157.15 |
| Domain Noise Cutoff | 157.15 |
| Isology Type | equivalog |
| EC Number | 6.1.1.20 |
| HMM Length | 451 |
| Mainrole Category | Protein synthesis |
| Subrole Category | tRNA aminoacylation |
| Gene Ontology Term | GO:0004826: phenylalanine-tRNA ligase activity molecular_function |
| | GO:0005739: mitochondrion cellular_component |
| | GO:0006432: phenylalanyl-tRNA aminoacylation biological_process |
| | GO:0009328: phenylalanine-tRNA ligase complex cellular_component |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:09PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This HMM models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. |
| References | A2 hmmalign
RM Medline; 92020858;
SE TIGR
GA hmmls
AL clustalw
BD 0528 |
