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
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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.
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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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[Homology]
Score
cysSCysteinyl-tRNA synthetase. (476 aa)    
Predicted Functional Partners:
MMP1240
Conserved hypothetical protein; Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)); Belongs to the SepCysS family.
   
 
 0.969
aEF-1
Translation elongation factor EF-1, subunit alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
   
 
 0.968
sepS
Phenylalanyl-tRNA synthetase alpha subunit; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
  
  
 0.950
thrS
Threonyl-tRNA synthetase; 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 edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase 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).
 
 
 0.929
leuS
Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.917
ileS
Isoleucyl-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.
 
  
 0.913
aspS
Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
 
  
 0.909
hisS
histidyl-tRNA synthetase; Citation: J Biol Chem 1985 Aug 25;260(18):10063-8; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.906
tyrS
Tyrosyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.
 
 
 0.905
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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