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
argSTIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; KEGG: hut:Huta_2012 arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (642 aa)    
Predicted Functional Partners:
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 2 subfamily.
 
 0.915
thrS
KEGG: hla:Hlac_1764 threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; TGS; Anticodon-binding; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.902
leuS
TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic; KEGG: hbo:Hbor_27430 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.828
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
  
  
 0.825
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.
 
 0.821
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).
 
 0.815
guaAB
GMP synthase (glutamine-hydrolyzing) subunit B; Catalyzes the synthesis of GMP from XMP.
   
  
 0.813
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).
 
 0.767
valS
Valyl-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 2 subfamily.
 
  
 0.747
infB
Translation initiation factor aIF-2; Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2.
 
  
 0.736
Your Current Organism:
halophilic archaeon DL31
NCBI taxonomy Id: 756883
Other names: h. archaeon DL31
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