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MSR1 protein (Saccharomyces cerevisiae) - STRING interaction network
"MSR1" - Mitochondrial arginyl-tRNA synthetase in Saccharomyces cerevisiae
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
MSR1Mitochondrial arginyl-tRNA synthetase (643 aa)    
Predicted Functional Partners:
GLN4
Glutamine tRNA synthetase, monomeric class I tRNA synthetase that catalyzes the specific glutaminylation of tRNA(Glu); N-terminal domain proposed to be involved in enzyme-tRNA interactions (809 aa)
   
 
  0.995
ILS1
Cytoplasmic isoleucine-tRNA synthetase, target of the G1-specific inhibitor reveromycin A (1072 aa)
 
 
  0.990
MES1
Methionyl-tRNA synthetase, forms a complex with glutamyl-tRNA synthetase (Gus1p) and Arc1p, which increases the catalytic efficiency of both tRNA synthetases; also has a role in nuclear export of tRNAs; Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction- methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met) (751 aa)
   
 
  0.988
GUS1
Glutamyl-tRNA synthetase (GluRS), forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl- tRNA(Gln) substrate for the tRNA-dependent amid [...] (708 aa)
   
 
  0.980
ISM1
Mitochondrial isoleucyl-tRNA synthetase, null mutant is deficient in respiratory growth (1002 aa)
   
 
  0.975
MSE1
Mitochondrial glutamyl-tRNA synthetase, predicted to be palmitoylated; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (536 aa)
   
 
  0.974
ARC1
Protein that binds tRNA and methionyl- and glutamyl-tRNA synthetases (Mes1p and Gus1p), delivering tRNA to them, stimulating catalysis, and ensuring their localization to the cytoplasm; also binds quadruplex nucleic acids; Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded r [...] (376 aa)
   
 
  0.971
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
   
 
  0.971
MSF1
Mitochondrial phenylalanyl-tRNA synthetase, active as a monomer, unlike the cytoplasmic subunit which is active as a dimer complexed to a beta subunit dimer; similar to the alpha subunit of E. coli phenylalanyl-tRNA synthetase; Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation (469 aa)
   
 
  0.968
MSM1
Mitochondrial methionyl-tRNA synthetase (MetRS), functions as a monomer in mitochondrial protein synthesis; functions similarly to cytoplasmic MetRS although the cytoplasmic form contains a zinc-binding domain not found in Msm1p (575 aa)
   
 
  0.966
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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