Protein Family Models

This is a highly divergent 3' exoribonuclease family. The proteins constitute a typical RNase fold, where the active site residues form a magnesium catalytic centre. The protein of the solved structure readily cleaves 3' overhangs in a time-dependent manner. It is similar to DEDD-type RNases and is an unusual ATP-binding protein that binds ATP and dATP. It forms a dimer in solution and both protomers in the asymmetric unit bind a magnesium ion through Asp-6 in SwissProt:P9WJ73 [1]. Proteins containing this domain also include 3'-5' exonuclease dexA from bacteriophage T4. It may play a role in the final step of host DNA degradation, by scavenging DNA into mononucleotides [2,3]. [1]. 24311791. Mycobacterium tuberculosis Rv2179c protein establishes a new. exoribonuclease family with broad phylogenetic distribution.. Abendroth J, Ollodart A, Andrews ES, Myler PJ, Staker BL,. Edwards TE, Arcus VL, Grundner C;. J Biol Chem. 2014;289:2139-2147.. [2]. 10581261. Role of exonucleolytic degradation in group I intron homing in. phage T4.. Huang YJ, Parker MM, Belfort M;. Genetics. 1999;153:1501-1512.. [3]. 3056918. Effect of DNA sequence and structure on nuclease activity of the. DexA protein of bacteriophage T4.. Gruber H, Kern G, Gauss P, Gold L;. J Bacteriol. 1988;170:5830-5836. (from Pfam)

Date:

2024-08-14

This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.; [1]. 8506149. RNase T shares conserved sequence motifs with DNA proofreading. exonucleases.. Koonin EV, Deutscher MP;. Nucleic Acids Res 1993;21:2521-2522. (from Pfam)

Date:

2024-08-14

3'-5' exonuclease similar to DNA polymerase III subunit epsilon, which is a proofreading 3'-5' exonuclease and contains the editing function of the multichain enzyme responsible for most of the replicative synthesis in bacteria

Date:

2023-02-24