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Mvol_0135 protein (Methanococcus voltae) - STRING interaction network
"Mvol_0135" - TIGRFAM: Asp/Glu amidotransferase, subunit C in Methanococcus voltae
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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:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
Mvol_0135TIGRFAM- Asp/Glu amidotransferase, subunit C (79 aa)    
Predicted Functional Partners:
gatA
Glutamyl-tRNA(Gln) amidotransferase subunit A; 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) (433 aa)
   
  0.993
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 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 (468 aa)
   
  0.993
aspS
Aspartate--tRNA(Asp/Asn) ligase; 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) (438 aa)
     
  0.971
dapA
4-hydroxy-tetrahydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta- semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- tetrahydrodipicolinate (HTPA) (288 aa)
              0.835
rps17e
30S ribosomal protein S17e; KEGG- AGAP004887-PA; K02962 small subunit ribosomal protein S17e; Belongs to the eukaryotic ribosomal protein eS17 family (65 aa)
              0.833
gatD
Glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate (450 aa)
       
    0.806
gatE
Glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate (645 aa)
         
    0.800
topA
DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (828 aa)
         
  0.703
Mvol_1254
KEGG- ech-ECH_0914 phosphomethylpyrimidine kinase; PFAM- Phosphomethylpyrimidine kinase type-1; Phosphomethylpyrimidine kinase (558 aa)
              0.684
Mvol_0940
TIGRFAM- asparagine synthase (glutamine-hydrolyzing); KEGG- wbr-WGLp587 asparagine synthetase B; PFAM- asparagine synthase; glutamine amidotransferase class-II (563 aa)
         
  0.624
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3
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