STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
valSvalyl-tRNA synthetase (valS); 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 2 subfamily. (878 aa)    
Predicted Functional Partners:
thrS
threonyl-tRNA synthetase (thrS); Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine, but does not detectably transfer it to tRNA(Thr). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain. Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl- tRNA(Thr). Deacylates correctly charged glycyl- tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor [...]
 
  
 0.975
ileS
isoleucyl-tRNA synthetase (ileS); 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.
 
 
0.964
leuS
leucyl-tRNA synthetase (leuS); Similar to SP:P26637 PID:1370340 PID:1403549 PID:3508 percent identity: 35.17; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.956
argS
arginyl-tRNA synthetase (argS); Identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.949
alaS
alanyl-tRNA synthetase (alaS); 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) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala).
 
  
 0.929
gltX
glutamyl-tRNA synthetase (gltX); 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).
 
 
 0.927
tyrS
tyrosyl-tRNA synthetase (trS); Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
  
  
 0.914
MJ_1130
O-sialoglycoprotein endopeptidase (gcp); Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction (By similarity). The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does [...]
 
  
 0.903
hisS
histidyl-tRNA synthetase (hisS); Similar to SP:P30053 percent identity: 35.44; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.882
serS
seryl-tRNA synthetase (serS); 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).
  
  
 0.856
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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