MSE1/YOL033W Summary Help

Standard Name MSE1 1
Systematic Name YOL033W
Feature Type ORF, Verified
Description Mitochondrial glutamyl-tRNA synthetase; predicted to be palmitoylated (1, 2 and see Summary Paragraph)
Name Description Mitochondrial aminoacyl-tRNA Synthetase, Glutamate (E) 1
Chromosomal Location
ChrXV:263475 to 265085 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All MSE1 GO evidence and references
  View Computational GO annotations for MSE1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 1 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
repressible
unspecified
Resources
12 total interaction(s) for 9 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Protein-peptide: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 2

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

Resources
Expression Summary
histogram
Resources
Length (a.a.) 536
Molecular Weight (Da) 61,603
Isoelectric Point (pI) 9.75
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXV:263475 to 265085 | 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..1611 263475..265085 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 SGDIDS000005393
SUMMARY PARAGRAPH for MSE1

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 MSE1
1) Tzagoloff A and Shtanko A  (1995) Mitochondrial and cytoplasmic isoleucyl-, glutamyl- and arginyl-tRNA synthetases of yeast are encoded by separate genes. Eur J Biochem 230(2):582-6
2) Ren J, et al.  (2008) CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng Des Sel 21(11):639-44
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