Accession | TIGR01125 |
Name | TIGR01125 |
Function | ribosomal protein S12 methylthiotransferase RimO |
Gene Symbol | rimO |
Trusted Cutoff | 356.95 |
Domain Trusted Cutoff | 356.95 |
Noise Cutoff | 332.15 |
Domain Noise Cutoff | 332.15 |
Isology Type | equivalog |
EC Number | 2.1.1.- 2.8.1.- |
HMM Length | 432 |
Mainrole Category | Protein synthesis |
Subrole Category | tRNA and rRNA base modification |
Gene Ontology Term | GO:0006400: tRNA modification biological_process |
| GO:0016782: transferase activity, transferring sulfur-containing groups molecular_function |
Author | Haft DH, Selengut J |
Entry Date | Jan 16 2001 2:22PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Members of this protein are the methylthiotransferase RimO, which modifies a conserved Asp residue in ribosomal protein S12. This clade of radical SAM family proteins is closely related to the tRNA modification bifunctional enzyme MiaB (see TIGR01574), and it catalyzes the same two types of reactions: a radical-mechanism sulfur insertion, and a methylation of the inserted sulfur. This clade spans alpha and gamma proteobacteria, cyano bacteria, Deinococcus, Porphyromonas, Aquifex, Helicobacter, Campylobacter, Thermotoga, Chlamydia, Streptococcus coelicolor and Clostridium, but does not include most other gram positive bacteria, archaea or eukaryotes. |
References | RN [1]
RM PMID:19736993
RT Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily.
RA Lee KH, Saleh L, Anton BP, Madinger CL, Benner JS, Iwig DF, Roberts RJ, Krebs C, Booker SJ
RL Biochemistry. 2009 Oct 27;48(42):10162-74.
RN [2]
RM PMID:20007320
RT Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical-SAM methylthiotransferase.
RA Arragain S, Garcia-Serres R, Blondin G, Douki T, Clemancey M, Latour JM, Forouhar F, Neely H, Montelione GT, Hunt JF, Mulliez E, Fontecave M, Atta M
RL J Biol Chem. 2009 Dec 9. |