YHR020W Summary Help

Systematic Name YHR020W
Feature Type ORF, Verified
Description Prolyl-tRNA synthetase; N-terminal domain shows weak homology to prokaryotic posttransfer editing domain, but does not possess posttransfer editing activity; may interact with ribosomes, based on co-purification experiments (1, 2, 3, 4 and see Summary Paragraph)
Chromosomal Location
ChrVIII:143996 to 146062 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All YHR020W GO evidence and references
  View Computational GO annotations for YHR020W
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 13 genes
Resources
Classical genetics
conditional
null
Large-scale survey
conditional
null
overexpression
repressible
Resources
94 total interaction(s) for 84 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 39
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 1
  • Co-purification: 1

Genetic Interactions
  • Negative Genetic: 44
  • Positive Genetic: 5
  • Synthetic Growth Defect: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 688
Molecular Weight (Da) 77,386
Isoelectric Point (pI) 6.36
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVIII:143996 to 146062 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2067 143996..146062 2011-02-03 1996-07-31
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 SGDIDS000001062
SUMMARY PARAGRAPH for YHR020W

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 (5, 6 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 (5, 6, 7 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for YHR020W
1) Tatusov RL, et al.  (2000) The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res 28(1):33-6
2) Fleischer TC, et al.  (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev 20(10):1294-307
3) Sternjohn J, et al.  (2007) Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain. Proc Natl Acad Sci U S A 104(7):2127-32
4) Hati S, et al.  (2006) Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids. J Biol Chem 281(38):27862-72
5) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
6) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
7) 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