Protein Family Models

This family contains proteins related to Pfam:PF02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity. (from Pfam)

Date:

2024-08-14

Members of this family are bacterial and archaeal RNA ligases that are able to ligate tRNA half molecules containing 2',3'-cyclic phosphate and 5' hydroxyl termini to products containing the 2',5' phosphodiester linkage. Each member of this family contains an internal duplication, each of which contains an HXTX motif that defines the family. The structure of a related protein is known [1]. They belong to the 2H phosphoesterase superfamily [2]. They share a common active site, characterised by two conserved histidines, with vertebrate myelin-associated 2',3' phosphodiesterases, plant Arabidopsis thaliana CPDases and several several bacteria and virus proteins. [1]. 11080166. Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction. Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A;. EMBO J 2000;19:6207-6217. [2]. 12466548. Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Mazumder R, Iyer LM, Vasudevan S, Aravind L;. Nucleic Acids Res 2002;30:5229-5243. (from Pfam)

Date:

2024-10-16

2'-5' RNA ligase family protein such as RNA 2',3'-cyclic phosphodiesterase hydrolyzes RNA 2',3'-cyclic phosphodiester to the RNA 2'-phosphomonoester

Date:

2018-01-17

Catalyzes the ligation and cleavage of of 2'-5' linkages in RNA

Gene:

thpR

Date:

2021-10-15

ThpR (two-histidine 2',3'-cyclic phosphodiesterase acting on RNA) was formerly named LigT, and called a 2'-5' RNA ligase, based on its ability to perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The more recent characterization in PMID:25239919 clarifies the likely biological role.

Gene:

thpR

Date:

2022-03-28