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Prior-Knowledge Description Expectation Prediction Conclusion Leaf Statistics
Component_42720 glutamyl-tRNA(Gln) amidotransferase, A subunit None - {{∅}} True - {{t}} Unconfirmed presence
Component_42721 glutamyl-tRNA(Gln) amidotransferase, B subunit None - {{∅}} True - {{t}} Unconfirmed presence
Component_42722 glutamyl-tRNA(Gln) amidotransferase, C subunit None - {{∅}} True - {{t}} Unconfirmed presence
Evidence_55090 TIGR00132 HMM None - {{∅}} True - {{t}} Unconfirmed presence
Evidence_55094 PF02686 HMM None - {{∅}} True - {{t}} Unconfirmed presence
Evidence_55093 PF01162 HMM None - {{∅}} None - {{∅}} Unexplained
Evidence_55092 TIGR00135 HMM None - {{∅}} True - {{t}} Unconfirmed presence
GenProp0188 GatABC aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase complex~The GatABC heterotrimer acts as an alternative to direct aminoacylation of tRNA(Gln), tRNA(Asn), or both with its respective amino acid. Rather, the tRNA may be misacylated with Glu in the place of Gln, or Asp in the place of Asn. The phylogenetic ranges over which GatABC orthologs act on Glu-tRNA(Gln), Asp-tRNA(Asn), or both are not fully worked out. It is both in Chlamydia, the Thermus-Deinococcus lineage, and Acidithiobacillus ferrooxidans. In the Archaea, GatDE act on Glu-tRNA(Gln) while GatABC act on Asp-tRNA(Asn). In Lactobacillus and possibly all Firmicutes, GatABC acts on Glu-tRNA(Gln) only. Note that the amidotransferase reaction is a mechanism not only to charge a tRNA with Asn or Gln, but to complete the synthesis of that amino acid. None - {{∅}} True - {{t}} Unconfirmed presence
Evidence_55091 TIGR00133 HMM None - {{∅}} True - {{t}} Unconfirmed presence