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gatE protein (Thermoproteus tenax) - STRING interaction network
"gatE" - glutamyl-tRNA(Gln) amidotransferase subunit E in Thermoproteus tenax
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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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gatEglutamyl-tRNA(Gln) amidotransferase subunit E; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate (610 aa)    
Predicted Functional Partners:
asnA
L-asparaginase; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate (415 aa)
     
  0.999
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis (118 aa)
       
    0.983
gatA
Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit (412 aa)
   
   
  0.934
NusG
Transcription antitermination protein nusG; Stimulates transcription elongation (162 aa)
   
     
  0.930
fusA
Elongation factor aEF-2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (740 aa)
   
     
  0.901
aspS
aspartyl-tRNA synthetase (430 aa)
 
   
  0.885
dph5
Diphthamide biosynthesis methyltransferase; S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF- 2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis (253 aa)
           
  0.856
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (432 aa)
           
  0.847
rgy
Reverse gyrase; Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5’ DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication (1223 aa)
 
     
  0.837
tfe
Transcription initiation factor E; Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation comple [...] (178 aa)
           
  0.801
Your Current Organism:
Thermoproteus tenax
NCBI taxonomy Id: 768679
Other names: T. tenax, T. tenax Kra 1, Thermoproteus tenax, Thermoproteus tenax DSM 2078, Thermoproteus tenax JCM 9277, Thermoproteus tenax Kra 1, Thermoproteus tenax str. Kra 1, Thermoproteus tenax strain Kra 1
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