A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications.

ABSTRACT: A protein family including mammalian NEMF, Drosophila caliban, yeast Tae2, and bacterial FpbA-like proteins was first defined over a decade ago and found to be universally distributed across the three domains/superkingdoms of life. Since its initial characterization, this family of proteins has been tantalizingly linked to a wide range of biochemical functions. Tapping the enormous wealth of genome information that has accumulated since the initial characterization of these proteins, we perform a detailed computational analysis of the family, identifying multiple conserved domains. Domains identified include an enzymatic domain related to the formamidopyrimidine (Fpg), MutM, and Nei/EndoVIII family of DNA glycosylases, a novel, predicted RNA-binding domain, and a domain potentially mediati

SUBMITTER: Burroughs AM 

PROVIDER: S-EPMC4075521 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature