FRS2/YFL022C Summary Help

Standard Name FRS2 1
Systematic Name YFL022C
Feature Type ORF, Verified
Description 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 (1, 2 and see Summary Paragraph)
Name Description phenylalanyl (F)-tRNA Synthetase 1
Gene Product Alias cytoplasmic phenylalanyl-tRNA synthetase alpha subunit 1
Chromosomal Location
ChrVI:95010 to 93499 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All FRS2 GO evidence and references
  View Computational GO annotations for FRS2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 5 genes
Resources
Large-scale survey
conditional
null
overexpression
reduction of function
Resources
32 total interaction(s) for 25 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-RNA: 3
  • Biochemical Activity: 1
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Growth Defect: 1
  • Synthetic Lethality: 5

Resources
Expression Summary
histogram
Resources
Length (a.a.) 503
Molecular Weight (Da) 57,511
Isoelectric Point (pI) 5.6
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVI:95010 to 93499 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 2011-02-03
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1512 95010..93499 2011-02-03 2011-02-03
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001872
SUMMARY PARAGRAPH for FRS2

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 FRS2
1) Sanni A, et al.  (1988) Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase. J Biol Chem 263(30):15407-15
2) Aphasizhev R, et al.  (1996) Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site. Biochemistry 35(1):117-23
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