| Type: | Domain | Name: | Thg1 C-terminal domain |
| Description: | Thg1 was originally characterised as synthesising the guanine nucleotide at the -1 position of the histidinyl tRNA (HtRNA). Thg1 has also been shown to have polymerase activity, which has been proposed to be the ancestral activity of this enzyme [, ]. Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands []. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site []. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA []. | Short Name: | Thg1_C_dom |
