| Accession | TIGR01579 |
| Name | MiaB-like-C |
| Function | MiaB-like tRNA modifying enzyme |
| Trusted Cutoff | 357.05 |
| Domain Trusted Cutoff | 357.05 |
| Noise Cutoff | 352.05 |
| Domain Noise Cutoff | 352.05 |
| Isology Type | hypoth_equivalog |
| HMM Length | 416 |
| Mainrole Category | Protein synthesis |
| Subrole Category | tRNA and rRNA base modification |
| Author | Selengut J |
| Entry Date | Jul 9 2002 1:01PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574 [1,2,3]).
Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate.
This clade is a member of a subfamily (TIGR00089) and spans low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium. |
| References | RN [1]
RM PMID: 10572129
RT Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli.
RA Esberg B, Leung HC, Tsui HC, Bjork GR, Winkler ME.
RL J Bacteriol. 1999 Dec;181(23):7256-65.
RN [2]
RM PMID: 11882645
RT Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.
RA Pierrel F, Bjork GR, Fontecave M, Atta M.
RL J Biol Chem. 2002 Apr 19;277(16):13367-70.
RN [3]
RM PMID: 11313137
RT TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.
RA Anantharaman V, Koonin EV, Aravind L.
RL FEMS Microbiol Lett. 2001 Apr 13;197(2):215-21. |
