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valS valS guaA guaA ileS ileS alaS alaS leuS leuS aspS aspS pheT pheT thrS thrS serS serS hisS hisS metG metG
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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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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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valSvalyl-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. (883 aa)    
Predicted Functional Partners:
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.923
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 1 subfamily.
 
 
0.915
alaS
alanyl-tRNA synthetase; 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.903
leuS
TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: dvl:Dvul_1861 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.902
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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.886
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: dvl:Dvul_0712 phenylalanyl-tRNA synthetase subunit beta.
  
  
 0.821
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).
 
  
 0.818
serS
seryl-tRNA synthetase; 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).
 
  
 0.803
hisS
TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: dvm:DvMF_2037 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding.
 
 
 0.802
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.
 
 
0.775
Your Current Organism:
Desulfovibrio alaskensis
NCBI taxonomy Id: 207559
Other names: D. alaskensis G20, Desulfovibrio alaskensis G20, Desulfovibrio alaskensis str. G20, Desulfovibrio alaskensis strain G20, Desulfovibrio desulfuricans subsp. desulfuricans str. G20
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