Light-oxygen-voltage sensitive (LOV) flavoproteins are ubiquitous photoreceptors
First-pass extracted concept
LOV domain photoreceptors
Aliases
candidate LOV domains, Light-oxygen-voltage sensitive (LOV) flavoproteins, LOV flavoproteins
Evidence Snippets
Supporting Sources
Linked Claims
The study bioinformatically identified over 6,700 candidate LOV domains, including over 4,000 previously unidentified sequences from plants and protists.
Here, we report the bioinformatics identification of over 6,700 candidate LOV domains (including over 4,000 previously unidentified sequences from plants and protists)
LOV proteins show a surprisingly high prevalence of effectors with functions previously thought to be rare, including regulators of G protein signaling, and include previously unidentified effectors such as lipases.
We found a surprisingly high prevalence of effectors with functions previously thought to be rare among LOV proteins, such as regulators of G protein signaling, and discovered several previously unidentified effectors, such as lipases.
LOV flavoproteins are ubiquitous photoreceptors that mediate responses to environmental cues.
Light-oxygen-voltage sensitive (LOV) flavoproteins are ubiquitous photoreceptors that mediate responses to environmental cues.
Preserving sensor-effector orientation is suggested to be a key determinant of linker length in LOV signaling, in addition to ancestry.
This finding suggests that preserving sensor-effector orientation is a key determinant of linker length, in addition to ancestry, in LOV signaling structure-function.
Motif analysis identified LOV sensors from approximately 42 million ORFs with strong statistical separation from other flavoproteins and non-LOV PAS family members.
Motif analysis identified the sensors from 42 million ORFs, with strong statistical separation from other flavoproteins and non-LOV members of the structurally related Per-aryl hydrocarbon receptor nuclear translocator (ARNT)-Sim family.
For certain effectors, sensor-effector linker length is discretized based on both phylogeny and preservation of alpha-helical heptad repeats within an extended coiled-coil linker structure.
We found that for certain effectors, sensor-effector linker length is discretized based on both phylogeny and the preservation of b1-helical heptad repeats within an extended coiled-coil linker structure.