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tyrS protein (Methanococcus voltae) - STRING interaction network
"tyrS" - Tyrosine--tRNA ligase in Methanococcus voltae
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query proteins and first shell of interactors
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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tyrSTyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily (321 aa)    
Predicted Functional Partners:
tuf
Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (428 aa)
   
 
  0.944
ileS
Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile); Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily (1053 aa)
   
 
  0.860
metG
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (703 aa)
 
  0.852
alaS
Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (936 aa)
 
 
  0.838
hisS
Histidine--tRNA ligase; TIGRFAM- histidyl-tRNA synthetase; KEGG- hypothetical protein; K01892 histidyl-tRNA synthetase; PFAM- tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family (417 aa)
   
   
  0.824
eif1a
Translation initiation factor 1A; Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (104 aa)
 
   
  0.810
leuS
Leucine--tRNA ligase; KEGG- similar to leucyl-tRNA synthetase; K01869 leucyl-tRNA synthetase; TIGRFAM- leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (1000 aa)
 
   
  0.810
serS
Type-2 serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec); Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily (523 aa)
   
   
  0.797
gltX
Glutamate--tRNA ligase; 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) (574 aa)
 
   
  0.768
thrS
Threonine--tRNA ligase; KEGG- gbm-Gbem_1990 threonyl-tRNA synthetase; TIGRFAM- threonyl-tRNA synthetase; PFAM- Threonyl-tRNA synthetase editing domain protein; tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family (629 aa)
   
 
  0.757
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3
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