v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | This entry represents a three-layer alpha/beta/alpha domain found as the catalytic domain at the C-terminal in homotetrameric tRNA-intron endonucleases [ ], and as domains 2 and 4 (C-terminal) in the homodimeric enzymes []. tRNA-intron endonucleases () remove tRNA introns by cleaving pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-hydroxyl termini [ ]. These enzymes recognise a pseudosymmetric substrate in which two bulged loops of three bases are separated by a stem of four bp []. Although homotetrameric enzymes contain four active sites, only two participate in the cleavage, and should therefore, be considered as a dimer of dimers. |
Short Name | tRNA_intron_Endonuc_cat-like |