VAS1/YGR094W Summary Help

VAS1 BASIC INFORMATION

Standard Name VAS1
Systematic Name YGR094W
Feature Type ORF, Verified
Description Mitochondrial and cytoplasmic valyl-tRNA synthetase (1, 2 and see Summary Paragraph)
Name Description VAlyl-tRNA Synthetase
GO Annotations All VAS1 GO evidence and references
    View Computational GO annotations for VAS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All VAS1 Phenotype details and references
Classical genetics
overexpression
Large-scale survey
null
overexpression
Interactions VAS1 All interactions details and references
19 total interaction(s) for 16 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 14
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Biochemical Activity: 2
  • Two-hybrid: 1
Sequence Information
ChrVII:672190 to 675504 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2004-07-20 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..3315 672190..675504 2004-07-20 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000003326

VAS1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for VAS1

SUMMARY PARAGRAPH for VAS1

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 VAS1]

1) Chatton B, et al.  (1988) The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J Biol Chem 263(1):52-7
2) Jordana X, et al.  (1987) Structure of the yeast valyl-tRNA synthetase gene (VASI) and the homology of its translated amino acid sequence with Escherichia coli isoleucyl-tRNA synthetase. J Biol Chem 262(15):7189-94
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