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
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
leuSCandidate Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (891 aa)    
Predicted Functional Partners:
metG
Candidate methionyl-tRNA synthetase (Methionine--tRNA ligase); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.983
ileS
Candidate isoleucyl-tRNA synthetase (Isoleucine--tRNA ligase); Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 sub [...]
 
0.969
proS
Global RNA synthesis factor; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involve [...]
 
 0.956
rlpB
Candidate Rare lipoprotein B; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane; Belongs to the LptE lipoprotein family.
  
  
 0.946
pheT
Candidate phenylalanyl-tRNA synthetase beta subunit(Phenylalanine--tRNA ligase alpha subuniit); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.935
argS
Candidate Arginyl-tRNA synthetase.
  
 0.928
lysU
Candidate lysyl-tRNA synthetase (Lysine--tRNA ligase); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.923
gltX
Candidate glutamyl-tRNA synthetase (Glutamate--tRNA ligase); Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.916
valS
Candidate valyl-tRNA synthetase (Valine--tRNA ligase); Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
   
 
 0.876
thrS
Candidate threonyl-tRNA synthetase (Threonine--tRNA ligase); Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
 
 
 0.873
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
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