| Accession | TIGR00322 |
| Name | diphth2_R |
| Function | diphthamide biosynthesis enzyme Dph1/Dph2 domain |
| Trusted Cutoff | 35.00 |
| Domain Trusted Cutoff | 35.00 |
| Noise Cutoff | 25.00 |
| Domain Noise Cutoff | 25.00 |
| Isology Type | domain |
| HMM Length | 320 |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:07PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (PF04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM. |
| References | RN [1]
RM PMID:20559380
RT Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.
RA Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H
RL Nature. 2010 Jun 17;465(7300):891-6. |
