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.
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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
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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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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:
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.
  
 
0.971
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 [...]
 
 
 0.970
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.
 
 
 0.956
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.
 
 
0.952
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 [...]
 
  
 0.932
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).
 
  
 0.931
argS
arginyl-tRNA synthetase (argS); Identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.928
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).
 
 
 0.912
pheS
phenylalanyl-tRNA synthetase, subunit alpha (pheS); Similar to SP:P15625 PID:172947 PID:836732 percent identity: 40.91; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
 
  
 0.895
rps3
SSU ribosomal protein S3P (rpsC); Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
 
  
 0.893
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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