Ontology highlight
ABSTRACT:
SUBMITTER: Lee BC
PROVIDER: S-EPMC3099691 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Lee Byung Cheon BC Lobanov Alexey V AV Marino Stefano M SM Kaya Alaattin A Seravalli Javier J Hatfield Dolph L DL Gladyshev Vadim N VN
The Journal of biological chemistry 20110310 21
Selenocysteine (Sec) residues occur in thiol oxidoreductase families, and functionally characterized selenoenzymes typically have a single Sec residue used directly for redox catalysis. However, how new Sec residues evolve and whether non-catalytic Sec residues exist in proteins is not known. Here, we computationally identified several genes with multiple Sec insertion sequence (SECIS) elements, one of which was a methionine-R-sulfoxide reductase (MsrB) homolog from Metridium senile that has fou ...[more]