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gatA gatA gatC gatC gatB gatB asnS asnS glnS glnS aspS aspS guaA guaA carB carB gltX gltX Dde_2004 Dde_2004 pyrB pyrB
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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gatAglutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (487 aa)    
Predicted Functional Partners:
gatC
glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 0.999
gatB
glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 0.999
asnS
TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type.
   
 0.979
glnS
TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain.
  
 0.977
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.
  
 
 0.853
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
 
 0.846
carB
SMART: MGS-like; TIGRFAM: Carbamoyl phosphate synthase, large subunit, glutamine-dependent; KEGG: dvm:DvMF_2306 carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl phosphate synthetase, large subunit, ATP-binding; Carbamoyl phosphate synthetase, large subunit, oligomerisation; MGS-like; Carbamoyl phosphate synthase, large subunit, N-terminal; Belongs to the CarB family.
  
 
 0.805
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).
  
 
 0.781
Dde_2004
PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; KEGG: dvu:DVU1693 glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.762
pyrB
TIGRFAM: Aspartate carbamoyltransferase, eukaryotic; KEGG: dvm:DvMF_1425 aspartate carbamoyltransferase catalytic subunit; PFAM: Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding; Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
  
    0.608
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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