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
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. (883 aa)    
Predicted Functional Partners:
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.916
Taci_0949
TIGRFAM: FolC bifunctional protein; PFAM: cytoplasmic peptidoglycan synthetase domain protein; Mur ligase middle domain protein; KEGG: gbm:Gbem_3348 FolC bifunctional protein; Belongs to the folylpolyglutamate synthase family.
 
  
 0.909
ileS
isoleucyl-tRNA synthetase; 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 subfamily.
 
 
0.905
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: ppd:Ppro_1731 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.868
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.
  
  
 0.856
Taci_0948
PFAM: protein of unknown function DUF152; KEGG: bpe:BP1148 hypothetical protein.
       0.825
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.
 
  
 0.799
thrS
KEGG: dde:Dde_2639 threonyl-tRNA synthetase / Ser- tRNA(Thr) hydrolase; TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
  
 0.795
glyS
KEGG: pca:Pcar_0599 glycine tRNA synthetase, beta subunit; TIGRFAM: glycyl-tRNA synthetase, beta subunit.
  
  
 0.790
lon
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
  
 0.777
Your Current Organism:
Thermanaerovibrio acidaminovorans
NCBI taxonomy Id: 525903
Other names: T. acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans str. DSM 6589, Thermanaerovibrio acidaminovorans strain DSM 6589
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.