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rimO protein (Methylobacter tundripaludum) - STRING interaction network
"rimO" - Ribosome maturation factor RimO in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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rimORibosome maturation factor RimO ; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12 (436 aa)    
Predicted Functional Partners:
rlmN
tRNA m2A37 methyltransferase ; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity (370 aa)
   
   
  0.650
guaA
Glutamine amidotransferase ; Catalyzes the synthesis of GMP from XMP (528 aa)
   
        0.640
dusA
tRNA-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)
   
   
  0.631
Mettu_3601
Heat shock protein 70 (432 aa)
   
 
  0.625
Mettu_1869
Inosine-5’-monophosphate dehydrogenase (488 aa)
   
        0.619
dnaJ
Chaperone protein DnaJ ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] (376 aa)
   
      0.609
Mettu_3235
DnaK-related protein (646 aa)
   
 
  0.597
dnaK
Heat shock protein 70 ; Acts as a chaperone (644 aa)
   
 
  0.597
Mettu_0186
Putative chaperone heat-shock protein (932 aa)
   
 
  0.597
dusB
tRNA-dihydrouridine synthase B ; 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 (327 aa)
   
   
  0.590
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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