THS1/YIL078W Summary 
THS1 BASIC INFORMATION
| Standard Name | THS1 |
|---|---|
| Systematic Name | YIL078W |
| Feature Type | ORF, Verified |
| Description | Threonyl-tRNA synthetase, essential cytoplasmic protein (1 and see Summary Paragraph) 
|
| Name Description | THreonyl tRNA Synthetase |
| Gene Product Alias | threonyl-tRNA synthetase 1 |
| GO Annotations | All THS1 GO evidence and references |
|---|---|
| View Computational GO annotations for THS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Mutant Phenotype | All THS1 Phenotype details and references |
|---|---|
| Large-scale survey | |
| null |
| Interactions | THS1 All interactions details and references |
|---|---|
| 23 total interaction(s) for 22 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000001340 |
|---|
THS1 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
|
Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for THS1
SUMMARY PARAGRAPH for THS1
THS1 encodes cytoplasmic threonyl-tRNA synthetase, the aminoacyl-tRNA synthetase specific for threonine (1). This enzyme is highly conserved across organisms and has extensive amino acid similarity with both the human and Escherichia coli threonyl-tRNA synthetases (2).
In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (3, 4 and references therein).
Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (3, 4, 5 and references therein).
Last updated: 2008-07-14
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for THS1]
| 1) | Pape LK and Tzagoloff A (1985) Cloning and characterization of the gene for the yeast cytoplasmic threonyl-tRNA synthetase. Nucleic Acids Res 13(17):6171-83 |
| 2) | Cruzen ME and Arfin SM (1991) Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes. J Biol Chem 266(15):9919-23 |
| 3) | Delarue M (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55 |
| 4) | Arnez JG and Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6 |
| 5) | Eriani G, et al. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6 |
