| Primary Identifier | IPR038250 | Type | Homologous_superfamily |
| Short Name | TGT_C2_sf |
| description | Archaeosine tRNA-guanine transglycosylase (ArcTGT) is made of an N-terminal catalytic domain and a C-terminal region with unidentified functions. The C-terminal region is divided into three domains, C1, C2, and C3. The catalytic domain of TGT has conserved basic residues on the outer surface of the N-terminal three-stranded beta sheet, which closes the barrel. It is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds [].This superfamily represents domain C2 of ArcTGT, formed by a four-stranded anti-parallel β-sheet lined with two alpha helices. It has conserved basic residues on the surface of the β-sheets as does the C-terminal domain PUA () []. |
