| 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 the archaea and eukaryotes. The only archaeal miaB-like genes are in this clade, while eukaryotes have sequences described by this HMM as well as ones falling within the scope of the MiaB equivalog model. |
| 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. |
