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thiI protein (Methanococcus voltae) - STRING interaction network
"thiI" - Thiamine biosynthesis/tRNA modification protein ThiI in Methanococcus voltae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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thiIThiamine biosynthesis/tRNA modification protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS (429 aa)    
Predicted Functional Partners:
metG
methionyl-tRNA synthetase; 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)
         
  0.925
truB
rRNA pseudouridine synthase; Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (336 aa)
         
  0.904
pus10
THUMP domain-containing protein; Responsible for synthesis of pseudouridine from uracil- 54 and uracil-55 in the psi GC loop of transfer RNAs (519 aa)
         
  0.904
ksgA
Dimethyladenosine transferase; Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3’-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (275 aa)
   
   
  0.876
cysS
cysteinyl-tRNA synthetase (559 aa)
         
  0.808
Mvol_0030
Thiamine biosynthesis/tRNA modification protein ThiI (429 aa)
   
   
 
0.800
Mvol_1325
Pseudouridine synthase I, TruA, alpha/beta domain-containing protein (271 aa)
   
   
  0.785
Mvol_1635
Metalloendopeptidase, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function (575 aa)
   
   
  0.760
argG
Argininosuccinate synthase (399 aa)
   
   
  0.736
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP (127 aa)
         
  0.736
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae, M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3, Methanococcus voltaei
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