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Glu-tRNAGln amidotransferase C subunit
This is a family of Glu-tRNAGln amidotransferase C subunits. The Glu-tRNA Gln amidotransferase enzyme itself is an important translational fidelity mechanism replacing incorrectly charged Glu-tRNAGln with the correct Gln-tRANGln via transmidation of the misacylated Glu-tRNAGln [1,2]. This activity supplements the lack of glutaminyl-tRNA synthetase activity in gram-positive eubacterteria, cyanobacteria, Archaea, and organelles [1]. This entry includes the C subunit of the bacterial/archaeal aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferases and eukaryotic Glu-tRNAGln amidotransferases (GatC). [1]. 9342321. Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme. required for correct decoding of glutamine codons during. translation. Curnow AW, Hong Kw, Yuan R, Kim Si, Martins O, Winkler W, Henkin. TM, Soll D;. Proc Natl Acad Sci U S A 1997;94:11819-11826.. [2]. 25548166. Structure of the Pseudomonas aeruginosa transamidosome reveals. unique aspects of bacterial tRNA-dependent asparagine. biosynthesis.. Suzuki T, Nakamura A, Kato K, Soll D, Tanaka I, Sheppard K, Yao. M;. Proc Natl Acad Sci U S A. 2015;112:382-387. (from Pfam)
aspartyl/glutamyl-tRNA amidotransferase subunit C
aspartyl/glutamyl-tRNA synthase subunit C (GatC) is part of a heterotrimeric complex that forms correctly charged Gln-tRNA(Gln) or Asn-tRNA(Asn) through the transamidation of misacylated Glu-tRNA(Gln) or Asp-tRNA(Asn)
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC
Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this HMM does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This HMM has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model.
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