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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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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.
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co-expression
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valSvalyl-tRNA synthetase; 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. (927 aa)    
Predicted Functional Partners:
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.910
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.897
ileS
isoleucyl-tRNA synthase; 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).
  
 
 0.890
leuS
Pfam:pfam13603 Leucyl-tRNA synthetase, Domain 2; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
 
 0.886
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.878
thrS
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).
 
 
 0.857
pheT
phenylalanyl-tRNA synthetase subunit beta; Pfam:pfam03483 B3/4 domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.813
serS
seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec).
 
  
 0.803
glyS
Pfam:pfam02092 Glycyl-tRNA synthetase beta subunit.
  
  
 0.790
proS
proline--tRNA ligase; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.
  
 
 0.776
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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