Rattus_norvegicusFamily: tRNA_int_endo Number of Genes: 3
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
Tsen34
Tsen34l1
Tsen2

Introduction

Pfam

Members of this family cleave pre tRNA at the 5' and 3' splice sites to release the intron EC:3.1.27.9.

InterPro

This entry represents a three-layer alpha/beta/alpha domain found as the catalytic domain at the C-terminal in homotetrameric tRNA-intron endonucleases [PUBMED:9535656], and as domains 2 and 4 (C-terminal) in the homodimeric enzymes [PUBMED:16690865]. tRNA-intron endonucleases (EC) 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 [PUBMED:9200602]. These enzymes recognise a pseudosymmetric substrate in which two bulged loops of three bases are separated by a stem of four bp [PUBMED:14993668]. Although homotetrameric enzymes contain four active sites, only two participate in the cleavage, and should therefore, be considered as a dimer of dimers.

Reference

  1. Kleman-Leyer K, Armbruster DW, Daniels CJ; , Cell 1997;89:839-847.: Properties of H. volcanii tRNA intron endonuclease reveal a relationship between the archaeal and eucaryal tRNA intron processing systems. PUBMED:9200602 EPMC:9200602 .

  2. Li H, Trotta CR, Abelson J; , Science 1998;280:279-284.: Crystal structure and evolution of a transfer RNA splicing enzyme. PUBMED:9535656 EPMC:9535656 .

  3. Steczkiewicz K, Muszewska A, Knizewski L, Rychlewski L, Ginalski K;, Nucleic Acids Res. 2012;40:7016-7045.: Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily. PUBMED:22638584 EPMC:22638584.