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hisS protein (Methylobacter tundripaludum) - STRING interaction network
"hisS" - Histidyl-tRNA synthetase in Methylobacter tundripaludum
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hisSHistidyl-tRNA synthetase (424 aa)    
Predicted Functional Partners:
hisG
ATP phosphoribosyltransferase ; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N’-(5’-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (209 aa)
 
  0.958
serS
Seryl-tRNA(Ser/Sec) 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) (423 aa)
   
 
  0.942
leuS
Leucyl-tRNA synthetase (832 aa)
 
   
  0.925
pheT
Phenylalanyl-tRNA synthetase beta subunit (791 aa)
 
   
  0.920
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 (931 aa)
 
   
  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 (870 aa)
   
   
  0.902
lysS
Lysyl-tRNA synthetase (499 aa)
   
 
  0.900
thrS
Threonyl-tRNA synthetase (635 aa)
   
 
  0.898
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) (943 aa)
 
   
  0.888
Mettu_2700
Putative uncharacterized protein (213 aa)
   
        0.878
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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