THS1/YIL078W Summary Help

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
Chromosomal Location
ChrIX:212499 to 214703 | ORF Map | GBrowse
Gene Ontology 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
Regulators 6 genes
Large-scale survey
reduction of function
73 total interaction(s) for 64 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 25
  • Affinity Capture-RNA: 4
  • Biochemical Activity: 4
  • Protein-peptide: 1

Genetic Interactions
  • Negative Genetic: 29
  • Positive Genetic: 7
  • Synthetic Lethality: 3

Expression Summary
Length (a.a.) 734
Molecular Weight (Da) 84,520
Isoelectric Point (pI) 7.01
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIX:212499 to 214703 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1994-12-10
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2205 212499..214703 2011-02-03 1994-12-10
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001340

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).

About aminoacyl-tRNA synthetases...

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 Contact SGD

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