Central cellular functions such as metabolism, solute transport and signal transduction are regulated, in part, via binding of small molecules by specialised domains. The 4-vinyl reductase (4VR) domain is a predicted small molecular binding domain, that may bind to hydrocarbons [ (PUBMED:11292341) ]. Proteins that contain this domain include a regulator of the phenol catabolic pathway [ (PUBMED:9023219) ] and a protein involved in chlorophyll biosynthesis.
Family alignment:
There are 4380 V4R domains in 4333 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing V4R domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with V4R domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing V4R domain in the selected taxonomic class.
Cellular role (predicted cellular role)
Cellular role: metabolism Binding / catalysis: may bind to hydrocarbons
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Regulatory potential, phyletic distribution and evolution of ancient,intracellular small-molecule-binding domains.
J Mol Biol. 2001; 307: 1271-92
Display abstract
Central cellular functions such as metabolism, solute transport and signaltransduction are regulated, in part, via binding of small molecules byspecialized domains. Using sensitive methods for sequence profile analysisand protein structure comparison, we exhaustively surveyed the proteinsets from completely sequenced genomes for all occurrences of 21intracellular small-molecule-binding domains (SMBDs) that are representedin at least two of the three major divisions of life (bacteria, archaeaand eukaryotes). These included previously characterized domains such asPAS, GAF, ACT and ferredoxins, as well as three newly predicted SMBDs,namely the 4-vinyl reductase (4VR) domain, the NIFX domain and the3-histidines (3H) domain. Although there are only a limited number ofdifferent superfamilies of these ancient SMBDs, they are present innumerous distinct proteins combined with various enzymatic, transport andsignal-transducing domains. Most of the SMBDs show considerableevolutionary mobility and are involved in the generation of manylineage-specific domain architectures. Frequent re-invention of analogousarchitectures involving functionally related, but not homologous, domainswas detected, such as, fusion of different SMBDs to several types ofDNA-binding domains to form diverse transcription regulators inprokaryotes and eukaryotes. This is suggestive of similar selective forcesaffecting the diverse SMBDs and resulting in the formation of multidomainproteins that fit a limited number of functional stereotypes. Using the"guilt by association approach", the identification of SMBDs allowedprediction of functions and mode of regulation for a variety of previouslyuncharacterized proteins.
