Xiphophorus_couchianusFamily: tRNA_int_endo Number of Genes: 2
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
eif2a
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tsen2
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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.