Sm domain
IPR047575
Definition
This entry represents a domain found in Sm, Lsm (like-Sm) and Hfq proteins that belong to a large family of proteins from all cellular organisms and are involved in numerous processes associated with RNA processing and gene expression regulation. The Sm and Lsm proteins are found in archaea and eukaryotes, whereas Hfq proteins exist in bacteria and in the archaea Methanocaldococcus jannaschii. The eukaryotic Sm and Lsm proteins form heteroheptameric complexes and play essential roles in splicing and mRNA decapping. In contrast, prokaryotic Hfq proteins associate in homohexamers and are involved in post-transcriptional regulation of gene expression. Lsm archaeal proteins (SmAPs) form homoheptamers and interact with polynucleotide phosphorylase P and uridine-rich RNA sequences and are probably involved in the processing of tRNAs [[cite:PMID:11259661], [cite:PMID:12853626], [cite:PMID:23579284], [cite:PMID:33827399], [cite:PMID:33992715]]. All these proteins contain the Sm domain that spans ~60-70 residues in length and folds into an open five-stranded β-barrel capped on one side with an α-helix PMID:10025403. This domain contains two conserved sequence motifs, Sm1 and Sm2 PMID:7744013. The Sm domain is responsible for both protein oligomerisation and specific RNA binding.
28 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...