Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Alanine--tRNA ligase, mitochondrial; Cytoplasmic and mitochondrial alanyl-tRNA synthetase; required for protein synthesis; point mutation (cdc64-1 allele) causes cell cycle arrest at G1; lethality of null mutation is functionally complemented by human homolog AARS; mutations in human homolog AARS are associated with autoimmune disease polymyositis/dermatomyositis; Belongs to the class-II aminoacyl-tRNA synthetase family.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Asparagine--tRNA ligase, cytoplasmic; Cytosolic asparaginyl-tRNA synthetase; required for protein synthesis, catalyzes the specific attachment of asparagine to its cognate tRNA; Belongs to the class-II aminoacyl-tRNA synthetase family.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Serine--tRNA ligase, mitochondrial; Probable mitochondrial seryl-tRNA synthetase; mutant displays increased invasive and pseudohyphal growth; Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation; shares five highly conserved amino acids with human that when mutated cause leukoencephalopathy characterized by hypomyelination with brain stem and spinal cord involvement and leg spasticity (HBSL); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Beta subunit of cytoplasmic phenylalanyl-tRNA synthetase; forms a tetramer with Frs2p to generate active enzyme; able to hydrolyze mis-aminoacylated tRNA-Phe, which could contribute to translational quality control.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Alpha subunit of cytoplasmic phenylalanyl-tRNA synthetase; forms a tetramer with Frs1p to form active enzyme; evolutionarily distant from mitochondrial phenylalanyl-tRNA synthetase based on protein sequence, but substrate binding is similar; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Glycine--tRNA ligase 1, mitochondrial; Cytoplasmic and mitochondrial glycyl-tRNA synthase; ligates glycine to the cognate anticodon-bearing tRNA; transcription termination factor that may interact with the 3'-end of pre-mRNA to promote 3'-end formation; GRS1 has a paralog, GRS2, that arose from the whole genome duplication; human homolog GARS implicated in Charcot-Marie-Tooth disease, can complement yeast null mutant; Belongs to the class-II aminoacyl-tRNA synthetase family.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Glycine--tRNA ligase 2; Glycine-tRNA synthetase, not expressed under normal growth conditions; expression is induced under heat, oxidative, pH, or ethanol stress conditions; more stable than the major glycine-tRNA synthetase Grs1p at 37 deg C; GRS2 has a paralog, GRS1, that arose from the whole genome duplication.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Histidine--tRNA ligase, mitochondrial; Cytoplasmic and mitochondrial histidine tRNA synthetase; efficient mitochondrial localization requires both a presequence and an amino-terminal sequence; mutations in human ortholog HARS2 are associated with Perrault syndrome; Belongs to the class-II aminoacyl-tRNA synthetase family.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Lysine--tRNA ligase, cytoplasmic; Lysyl-tRNA synthetase.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Aspartate--tRNA ligase, mitochondrial; Mitochondrial aspartyl-tRNA synthetase; required for acylation of aspartyl-tRNA; yeast and bacterial aspartyl-, asparaginyl-, and lysyl-tRNA synthetases contain regions with high sequence similarity, suggesting a common ancestral gene.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Phenylalanine--tRNA ligase, mitochondrial; Mitochondrial phenylalanyl-tRNA synthetase; active as a monomer, unlike the cytoplasmic subunit which is active as a dimer complexed to a beta subunit dimer; similar to the alpha subunit of E. coli phenylalanyl-tRNA synthetase.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Lysine--tRNA ligase, mitochondrial; Mitochondrial lysine-tRNA synthetase; required for import of both aminoacylated and deacylated forms of tRNA(Lys) into mitochondria and for aminoacylation of mitochondrially encoded tRNA(Lys).

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Threonine--tRNA ligase, mitochondrial; Mitochondrial threonyl-tRNA synthetase; aminoacylates both the canonical threonine tRNA tT(UGU)Q1 and the unusual threonine tRNA tT(UAG)Q2 in vitro; lacks a typical editing domain, but has pre-transfer editing activity stimulated by the unusual tRNA-Thr.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Serine--tRNA ligase, cytoplasmic; Cytosolic seryl-tRNA synthetase; class II aminoacyl-tRNA synthetase that aminoacylates tRNA(Ser), displays tRNA-dependent amino acid recognition which enhances discrimination of the serine substrate, interacts with peroxin Pex21p.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Asparagine--tRNA ligase, mitochondrial; Mitochondrial asparaginyl-tRNA synthetase.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Threonine--tRNA ligase, cytoplasmic; Threonyl-tRNA synthetase; essential cytoplasmic protein; human homolog TARS can complement yeast null mutant.

Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.

Putative proline--tRNA ligase YHR020W; Prolyl-tRNA synthetase; N-terminal domain shows weak homology to prokaryotic posttransfer editing domain, but does not possess posttransfer editing activity; may interact with ribosomes, based on co-purification experiments.

Putative lipoate-protein ligase; required along with Lip2 and Lip5 for lipoylation of Lat1p and Kgd2p; similar to E. coli LplA; null mutant displays reduced frequency of mitochondrial genome loss; Belongs to the LplA family.

Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase; Biotin:apoprotein ligase; covalently modifies proteins with the addition of biotin, required for acetyl-CoA carboxylase (Acc1p) holoenzyme formation; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon; human homolog HLCS can complement yeast BPL1 mutant.