The Lsm14 N-terminal domain is a type of LSM domain found in Lsm14 proteins (also known as Rap55) [, ]and in the Saccharomyces cerevisiae homologue Scd6 []. The domain is also found in the human EDC3 protein (enhancer of mRNA-decapping protein 3) where it is fused to the the Rossmanoid YjeF-N domain []. In addition, both EDC3 and Scd6 are found fused to the FDF domain [, ].
This entry represents the N-terminal of the Lsm16 protein. Lsm16 (also known as enhancer of decapping-3 or EDC3) has been shown to be associated with an mRNA-decapping complex Dcp1-Dcp2, required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end. EDC3 is believed to be a scaffold for decapping complex formation [, ,]. It belongs to a family of Sm-like proteins that associate with RNA to form complexes involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures []. Lsm16 has, in addition to its N-terminal Sm-like domain, a C-terminal Yjef_N-type Rossmann fold domain of unknown function [].
