HMM Summary Page: TIGR01578

FunctionMiaB-like tRNA modifying enzyme, archaeal-type
Trusted Cutoff314.70
Domain Trusted Cutoff314.70
Noise Cutoff310.95
Domain Noise Cutoff310.95
Isology Typehypoth_equivalog
HMM Length421
Mainrole CategoryProtein synthesis
Subrole CategorytRNA and rRNA base modification
AuthorSelengut J
Entry DateJul 9 2002 11:25AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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.
ReferencesRN [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.