EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) domain () and the 4Fe-4S binding domain (). It contains a characteristic EKR sequence motif. The exact function of this domain is not known.
EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) domain () and the 4Fe-4S binding domain (). It contains a characteristic EKR sequence motif. The exact function of this domain is not known.
This domain, about 385 amino acids long, can have either of at least two types of C-terminal sorting signal. Members from Shewanella and allies have the rhombosortase target domain GlyGly-CTERM (), while members of the Bacteroidetes have the Por secretion system C-terminal domain (). Most other members lack any C-terminal extension, but in most of those, the normal signal sequence is replaced by a lipoprotein signal sequence. Member sequences show a region of local similarity to the LVIVD repeat sequence ().
This entry includes proteins from plants and bacteria. The plant members CHAPERONE-LIKE PROTEIN OF POR1 (CPP1) and Protein CHLOROPLAST J-LIKE DOMAIN 1 (CJD1) have a J-like domain and three transmembrane domains. CPP1 is an essential protein for chloroplast development, plays a role in the regulation of POR (light-dependent protochlorophyllide oxidoreductase) stability and function [, , ]. CJD1 may be involved in the regulation of the fatty acid metabolic process in chloroplasts, especially chloroplastic galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG) [].
