STRINGSTRING
STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
tilSHypothetical 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. (510 aa)    
Predicted Functional Partners:
KKB62272.1
Thiamine biosynthesis protein ThiS; With ThiF, ThiG, and ThiO catalyzes the formation of the thiazole moiety of thiamine pyrophosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.938
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
 
 0.869
tadA
CMP deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family.
 
 0.820
KKB61878.1
Hypoxanthine phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.802
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
  
  
 0.778
accA
acetyl-CoA carboxylase subunit alpha; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
      0.771
KKB64407.1
UDP-N-acetylglucosamine 2-epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
  
 
 0.769
KKB63831.1
UDP-N-acetylglucosamine 2-epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
  
 
 0.769
KKB64811.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the mannose-6-phosphate isomerase type 2 family.
    
  0.717
surE
Stationary phase survival protein SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
   
  0.679
Your Current Organism:
Robbsia andropogonis
NCBI taxonomy Id: 28092
Other names: ATCC 19311 [[Pseudomonas woodsii]], ATCC 23061, Aplanobacter stizolobii, Bacterium andropogoni, Bacterium woodsii, Burkholderia andropogonis, CCUG 32772, CFBP 2421, CIP 105771, DSM 9511, DSM 9884 [[Pseudomonas woodsii]], IBSBF 199, ICMP 2807, ICMP 3967 [[Pseudomonas woodsii]], JCM 10487, LMG 2129, LMG 2362 [[Pseudomonas woodsii]], LMG:2129, LMG:2362 [[Pseudomonas woodsii]], NCPPB 934, NCPPB 968 [[Pseudomonas woodsii]], NRRL B-14296, Paraburkholderia andropogonis, Pseudomonas andropogonis, Pseudomonas stizolobii, Pseudomonas woodsii, R. andropogonis, strain PW 102 [[Pseudomonas woodsii]]
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.