HMM Summary Page: TIGR01579

FunctionMiaB-like tRNA modifying enzyme
Trusted Cutoff357.05
Domain Trusted Cutoff357.05
Noise Cutoff352.05
Domain Noise Cutoff352.05
Isology Typehypoth_equivalog
HMM Length416
Mainrole CategoryProtein synthesis
Subrole CategorytRNA and rRNA base modification
AuthorSelengut J
Entry DateJul 9 2002 1:01PM
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 low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium.
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.