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thrS protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"thrS" - Threonine--tRNA ligase in Dermacoccus nishinomiyaensis
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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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thrSThreonine--tRNA ligase; Catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr); catalyzes a two-step reaction, first charging a threonine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family (665 aa)    
Predicted Functional Partners:
alaS
Alanine--tRNA ligase; 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 (904 aa)
   
 
  0.905
serS
Serine--tRNA ligase; 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) (437 aa)
 
 
  0.893
pheS
Phenylalanine--tRNA ligase alpha subunit; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (365 aa)
 
 
  0.881
leuS
Leucine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (956 aa)
 
 
  0.875
lysS
Lysine--tRNA ligase; Catalyzes a two-step reaction, first charging a lysine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family (1108 aa)
   
 
  0.871
ileS
Isoleucine--tRNA ligase; 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 (1138 aa)
 
 
  0.867
HX89_06765
HIT family hydrolase; Derived by automated computational analysis using gene prediction method- Protein Homology (177 aa)
 
   
  0.857
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (889 aa)
   
   
  0.850
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (704 aa)
   
 
  0.844
rpsE
30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body; Belongs to the universal ribosomal protein uS5 family (215 aa)
   
 
  0.836
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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