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ileS protein (Mycoplasma pulmonis) - STRING interaction network
"ileS" - Isoleucine--tRNA ligase in Mycoplasma pulmonis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ileSIsoleucine--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 1 subfamily (888 aa)    
Predicted Functional Partners:
pheT
Phenylalanine--tRNA ligase beta subunit; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (718 aa)
   
 
  0.977
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 (539 aa)
   
   
  0.933
cysS
Cysteine--tRNA ligase; Identified by sequence similarity; possible; similar to SWISS-PROT-P47495 (SYC_MYCGE) Blastp2 P=3e-63 C=36%; Belongs to the class-I aminoacyl-tRNA synthetase family (596 aa)
 
   
  0.923
leuS
leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase (807 aa)
   
 
0.923
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family (276 aa)
   
        0.915
pheS
Phenylalanine--tRNA ligase alpha subunit; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 1 subfamily; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (314 aa)
   
 
  0.909
valS
Valine--tRNA ligase; 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 (827 aa)
   
 
0.907
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 (873 aa)
   
 
  0.895
glyQS
Glycine--tRNA ligase; Catalyzes the attachment of glycine to tRNA(Gly); Belongs to the class-II aminoacyl-tRNA synthetase family (453 aa)
   
 
  0.893
tilS
tRNA(Ile)-lysidine synthase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine; Belongs to the tRNA(Ile)-lysidine synthase family (286 aa)
         
  0.871
Your Current Organism:
Mycoplasma pulmonis
NCBI taxonomy Id: 272635
Other names: M. pulmonis UAB CTIP, Mycoplasma pulmonis, Mycoplasma pulmonis UAB CTIP, Mycoplasma pulmonis str. UAB CTIP, Mycoplasma pulmonis strain UAB CTIP
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