This domain is found in nicking enzyme in S. aureus. NES initiates and terminates the transfer of plasmids that variously confer resistance to a range of drugs, including vancomycin and gentamicin. This domain is found in the C-terminal region of NES. The C-terminal region is required for conjugation and significantly impacts the catalytic activity of the N-terminal relaxase [].
CRM1 (also known as exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran.This entry represents the C-terminal domain of CRM1. It forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat [].
COP1 is a RING finger-type ubiquitin E3 ligase. In Arabidopsis, it is a central switch for the transition from plant growth underground in darkness (etiolation) to growth under light exposure (photomorphogenesis) []. In mammals, it functions as an E3 ubiquitin-protein ligase involved in tumorigenesis, gluconeogenesis, and lipid metabolism. It is regulated by the COP9 signalosome []and is involved in 14-3-3 delta ubiquitin-mediated degradation []. COP1 contains a classic leucine-rich NES and a novel bipartite NLS bridged by a RING finger domain [].
The transcription factor Yap1 is a central regulator of the response to oxidative stress in Saccharomyces cerevisiae. In the active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide-bond-mediated interactions with a conserved amino-terminal α-helix. Upon reduction of the disulphide bonds, Yap1 undergoes a change that exposes the NES and allows redistribution to the cytoplasm []. This entry represents a redox-regulated domain superfamily of Yap1.
