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dusA protein (Methylobacter tundripaludum) - STRING interaction network
"dusA" - tRNA-dihydrouridine synthase A in Methylobacter tundripaludum
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second shell of interactors
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proteins of unknown 3D structure
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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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dusAtRNA-dihydrouridine synthase A ; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs (331 aa)    
Predicted Functional Partners:
Mettu_4044
MscS Mechanosensitive ion channel (1136 aa)
       
      0.837
Mettu_3552
Probable transcriptional regulatory protein Mettu_3552 (248 aa)
     
   
  0.761
Mettu_3251
Probable transcriptional regulatory protein Mettu_3251 (238 aa)
     
   
  0.761
truB
tRNA-uridine isomerase ; Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (342 aa)
   
   
  0.731
truD
tRNA-uridine isomerase D ; Responsible for synthesis of pseudouridine from uracil- 13 in transfer RNAs (339 aa)
 
   
  0.696
birA
Biotin-[acetyl-CoA carboxylase] synthetase ; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5’-adenylate (BirA-bio- 5’-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon (332 aa)
              0.678
ttcA
tRNA 2-thiocytidine biosynthesis protein TtcA ; Required for the thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32) (284 aa)
 
   
  0.671
Mettu_2418
Nitrite and sulphite reductase 4Fe-4S region (550 aa)
       
      0.655
cysI
Sulfite reductase [NADPH] hemoprotein beta-component ; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L- cysteine from sulfate (573 aa)
       
      0.655
Mettu_2386
33 kDa chaperonin ; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (289 aa)
 
   
  0.645
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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