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ileS ileS leuS leuS pheT pheT proS proS argS argS gltX gltX metG metG trpS trpS tilS tilS lysU lysU valS valS
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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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colored nodes:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
ileSisoleucyl-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. (1052 aa)    
Predicted Functional Partners:
leuS
Similar to Escherichia coli leucyl-tRNA synthetase LeuS or B0642 SWALL:SYL_ECOLI (SWALL:P07813) (860 aa) fasta scores: E(): 1.9e-37, 37.53% id in 967 aa, and to Streptomyces coelicolor leucyl-tRNA synthetase LeuS SWALL:Q9RDL5 (EMBL:AL136518) (966 aa) fasta scores: E(): 1.6e-209, 59.93% id in 971 aa; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.990
pheT
Similar to Mycobacterium tuberculosis phenylalanyl-tRNA synthetase beta chain PheT or Rv1650 or MT1688 or MTCY06H11.15 SWALL:SYFB_MYCTU (SWALL:P94985) (831 aa) fasta scores: E(): 4.2e-156, 49.64% id in 844 aa, and to Bacillus subtilis phenylalanyl-tRNA synthetase beta chain PheT SWALL:SYFB_BACSU (SWALL:P17922) (804 aa) fasta scores: E(): 1.8e-53, 30.69% id in 847 aa.
  
 
 0.980
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 [...]
   
 0.978
argS
arginyl-tRNA synthetase; Similar to Mycobacterium tuberculosis arginyl-tRNA synthetase ArgS or Rv1292 or MT1331 or MTCY373.12 SW:SYR_MYCTU (Q10609) (550 aa) fasta scores: E(): 4.5e-144, 65.63% id in 550 aa, and to Bacillus subtilis arginyl-tRNA synthetase ArgS SW:SYR_BACSU (P46906) (556 aa) fasta scores: E(): 1.7e-82, 42.75% id in 545 aa.
  
 0.945
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.
 
 0.914
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.
  
 0.899
trpS
tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.862
tilS
Conserved hypothetical protein; 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.
     
 0.862
lysU
Putative lysyl-tRNA synthetase; Similar to Escherichia coli heat inducible lysyl-tRNA synthetase LysU SW:SYK2_ECOLI (P14825) (504 aa) fasta scores: E(): 4.5e-73, 40.8% id in 522 aa, and to Mycobacterium tuberculosis lysyl-tRNA synthetase 1 Rv3598c SW:SYK1_MYCTU (O06284) (505 aa) fasta scores: E(): 3.9e-118, 61.87% id in 522 aa; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.839
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 1 subfamily.
  
 
0.837
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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