Accession | TIGR01212 |
Name | TIGR01212 |
Function | radical SAM protein, TIGR01212 family |
Trusted Cutoff | 180.00 |
Domain Trusted Cutoff | 180.00 |
Noise Cutoff | 120.00 |
Domain Noise Cutoff | 120.00 |
Isology Type | hypoth_equivalog |
HMM Length | 302 |
Mainrole Category | Unknown function |
Subrole Category | Enzymes of unknown specificity |
Author | Haft DH |
Entry Date | Apr 3 2001 11:50AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | 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. |
References | RN [1]
RM PMID:20054296
RT A role for the elongator complex in zygotic paternal genome demethylation.
RA Okada Y, Yamagata K, Hong K, Wakayama T, Zhang Y
RL Nature. 2010 Jan 28;463(7280):554-8. doi: 10.1038/nature08732.
DR PFAM; PF04055 |