Protein Family Models

Both RNase E and its homologue RNase G are endoribonucleases that play central roles in RNA processing. RNase E shows two globular domains. This entry represents the smaller domain, which shows a thioredoxin-like fold [1-3]. Paper describing PDB structure 2bx2. [1]. 16237448. Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Callaghan AJ, Marcaida MJ, Stead JA, McDowall KJ, Scott WG, Luisi BF;. Nature. 2005;437:1187-1191. Paper describing PDB structure 2vmk. [2]. 18682225. The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Koslover DJ, Callaghan AJ, Marcaida MJ, Garman EF, Martick M, Scott WG, Luisi BF;. Structure. 2008;16:1238-1244. Paper describing PDB structure 5f6c. [3]. 30270108. Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E. Bandyra KJ, Wandzik JM, Luisi BF;. Mol Cell. 2018;72:275-285. (from Pfam)

Date:

2024-10-16

Ribonuclease E and Ribonuclease G are related enzymes that cleave a wide variety of RNAs [1]. [1]. 16237448. Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Callaghan AJ, Marcaida MJ, Stead JA, McDowall KJ, Scott WG, Luisi BF;. Nature. 2005;437:1187-1191. (from Pfam)

Date:

2024-10-16

The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure. Structure and an extension of S1 family. [1]. 9008164. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG;. Cell 1997;88:235-242. (from Pfam)

Date:

2024-10-16

Gene:

rng

Date:

2021-08-23

ribonuclease E and G are paralogs and are involved in rapid turnover of mRNA in bacteria

Date:

2017-02-03

This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome.

Date:

2024-05-16