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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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.
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experimentally determined
co-expression
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gene co-occurrence
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glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (462 aa)    
Predicted Functional Partners:
polA
5'-3' exonuclease, resolvase-like domain-containing protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
   
 0.785
leuS
KEGG: tit:Thit_0284 leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.766
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.
  
 
 0.748
proS
Prolyl-tRNA synthetase; 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 involves dea [...]
  
 
 0.733
argS
TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; KEGG: tbo:Thebr_0195 arginyl-tRNA synthetase.
  
 
 0.709
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.
  
 
 0.670
AEM78451.1
PFAM: Threonyl/alanyl tRNA synthetase, SAD; Alanyl-tRNA synthetase, class IIc, N-terminal; KEGG: tte:TTE0934 metal-dependent hydrolase.
  
 
 0.667
metG
Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 
 0.646
gltX
glutamyl-tRNA synthetase; 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.
  
 
 0.640
gltX-2
glutamyl-tRNA synthetase; 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.
  
 
 0.640
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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