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ileS ileS proS proS leuS leuS lysS lysS argS argS metG metG pheT pheT lspA lspA gltX gltX valS valS glnS glnS
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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[Homology]
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 1 subfamily. (940 aa)    
Predicted Functional Partners:
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 [...]
   
 0.993
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: son:SO1174 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.981
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; KEGG: shn:Shewana3_3296 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.978
argS
KEGG: shm:Shewmr7_0456 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase.
  
 0.970
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.
  
 0.966
pheT
KEGG: shm:Shewmr7_2168 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit.
  
 
 0.961
lspA
Signal peptidase II. Aspartic peptidase. MEROPS family A08; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
 
  
 0.942
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).
 
 0.934
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.
 
 
0.932
glnS
KEGG: shn:Shewana3_2669 glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase, class Ic.
  
 0.924
Your Current Organism:
Shewanella baltica
NCBI taxonomy Id: 325240
Other names: S. baltica OS155, Shewanella baltica OS155, Shewanella baltica str. OS155, Shewanella baltica strain OS155
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