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dusB dusB fis fis truB truB truA truA trmD trmD trmU trmU tilS tilS rluA rluA purH purH thiI thiI rnpA rnpA
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
dusBConserved hypothetical protein; 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; Belongs to the Dus family. DusB subfamily. (332 aa)    
Predicted Functional Partners:
fis
DNA-binding protein Fis; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the transcriptional regulatory Fis family.
  
  
 0.990
truB
tRNA pseudouridine 55 synthase; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity). Osmoprotectant regulator of PLC; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
  
  
 0.834
truA
tRNA-pseudouridine synthase I; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
  
 
 0.823
trmD
tRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
  
 0.820
trmU
tRNA methyltransferase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
  
  
 0.775
tilS
Conserved hypothetical protein; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family.
  
  
 0.757
rluA
Pseudouridine synthase RluA; Product name confidence: Class 2 (High similarity to functionally studied protein).
     
 0.738
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Product name confidence: Class 2 (High similarity to functionally studied protein).
  
    0.668
thiI
Thiazole biosynthesis 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.
  
  
 0.666
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
   
    0.649
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 208964
Other names: P. aeruginosa PAO1, Pseudomonas aeruginosa PAO1, Pseudomonas sp. PAO1
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