STRINGSTRING
ileS ileS pheT pheT proS proS leuS leuS lysS lysS glnS glnS lspA lspA metG metG argS argS gltX gltX 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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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
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textmining
co-expression
protein homology
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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. (938 aa)    
Predicted Functional Partners:
pheT
KEGG: ypp:YPDSF_0722 phenylalanyl-tRNA synthetase beta chain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.965
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 [...]
  
 0.965
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: ypi:YpsIP31758_2926 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.943
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: kpn:KPN_03318 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.928
glnS
TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase class Ic; KEGG: yen:YE2977 glutaminyl-tRNA synthetase.
  
 0.924
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
 
  
 0.919
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.
  
0.918
argS
KEGG: ypp:YPDSF_1077 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase.
  
 0.917
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).
 
 0.887
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.
 
 
0.870
Your Current Organism:
Serratia proteamaculans
NCBI taxonomy Id: 399741
Other names: S. proteamaculans 568, Serratia proteamaculans 568, Serratia proteamaculans str. 568, Serratia proteamaculans strain 568
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