Protein Family Models

This domain is found as a C-terminal extension to a subset of Radical_SAM domains. It is found in archaeal, bacterial, fungal, plant and human proteins. (from Pfam)

Date:

2024-07-08

Radical SAM proteins catalyse diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. [1]. 11222759. Radical SAM, a novel protein superfamily linking unresolved. steps in familiar biosynthetic pathways with radical mechanisms:. functional characterization using new analysis and information. visualization methods.. Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE;. Nucleic Acids Res 2001;29:1097-1106.. [2]. 17335281. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able. to catalyze in vitro sulfatase post-translational modification.. Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O;. J Am Chem Soc. 2007;129:3462-3463.. [3]. 16766528. A new type of bacterial sulfatase reveals a novel maturation. pathway in prokaryotes.. Berteau O, Guillot A, Benjdia A, Rabot S;. J Biol Chem. 2006;281:22464-22470. (from Pfam)

Date:

2024-07-08

Members of this family are apparent radical-SAM enzymes, related to the N-terminal region of the bifunctional ELP3, whose C-terminal region is part of the elongator complex and appears to acetylate histones and other proteins. ELP3 binds S-adenosylmethionine (SAM) and was recently shown to be involved in a DNA demethylation process in eukaryotes. Close sequence similarity of this family (with lacks the GNAT family acetyltransferase domain) to the ELP3 N-terminal region and a strong match to the Pfam model PF04055 support identification of this family as radical SAM despite the atypical spacing between first and second Cys residues in the 4Fe4S-binding motif.

Date:

2024-06-27

TIGR01212 family radical SAM protein such as Bacillus subtilis protein YtqA that generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfer of a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Date:

2018-11-27