SES1/YDR023W Summary Help

Standard Name SES1 1
Systematic Name YDR023W
Feature Type ORF, Verified
Description 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 (2, 3, 4, 5, 6 and see Summary Paragraph)
Name Description SEryl-tRNA Synthetase 1
Gene Product Alias SerRS 3 , seryl-tRNA synthetase 3
Chromosomal Location
ChrIV:489508 to 490896 | ORF Map | GBrowse
Gene Ontology Annotations All SES1 GO evidence and references
  View Computational GO annotations for SES1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 1 genes
Large-scale survey
54 total interaction(s) for 46 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 21
  • Affinity Capture-RNA: 4
  • Biochemical Activity: 15
  • Reconstituted Complex: 3
  • Two-hybrid: 6

Genetic Interactions
  • Negative Genetic: 5

Expression Summary
Length (a.a.) 462
Molecular Weight (Da) 53,309
Isoelectric Point (pI) 5.98
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:489508 to 490896 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1389 489508..490896 2011-02-03 1996-07-31
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 SGDIDS000002430

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 (7, 8 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 (7, 8, 9 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for SES1
1) Weygand-Durasevic I, et al.  (1996) The C-terminal extension of yeast seryl-tRNA synthetase affects stability of the enzyme and its substrate affinity. J Biol Chem 271(5):2455-61
2) Lenhard B, et al.  (1997) Defining the active site of yeast seryl-tRNA synthetase. Mutations in motif 2 loop residues affect tRNA-dependent amino acid recognition. J Biol Chem 272(2):1136-41
3) Weygand-Durasevic I, et al.  (1987) Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiae. Nucleic Acids Res 15(5):1887-904
4) Lenhard B, et al.  (1998) C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition. FEBS Lett 439(3):235-40
5) Rocak S, et al.  (2002) Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase. FEMS Microbiol Lett 214(1):101-6
6) Gruic-Sovulj I, et al.  (2002) tRNA-dependent amino acid discrimination by yeast seryl-tRNA synthetase. Eur J Biochem 269(21):5271-9
7) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
8) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
9) 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