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MnmE helical domain
The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain [1-2]. [1]. 12730230. The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. Yim L, Martinez-Vicente M, Villarroya M, Aguado C, Knecht E, Armengod ME;. J Biol Chem. 2003;278:28378-28387. [2]. 19806182. Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy. Meyer S, Bohme S, Kruger A, Steinhoff HJ, Klare JP, Wittinghofer A;. PLoS Biol. 2009;7:e1000212. (from Pfam)
GTP-binding protein TrmE N-terminus
This family represents the shorter, B, chain of the homo-dimeric structure which is a guanine nucleotide-binding protein that binds and hydrolyses GTP. TrmE is homologous to the tetrahydrofolate-binding domain of N,N-dimethylglycine oxidase and indeed binds formyl-tetrahydrofolate. TrmE actively participates in the formylation reaction of uridine and regulates the ensuing hydrogenation reaction of a Schiff's base intermediate. This B chain is the N-terminal portion of the protein consisting of five beta-strands and three alpha helices and is necessary for mediating dimer formation within the protein [1]. [1]. 15616586. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. Scrima A, Vetter IR, Armengod ME, Wittinghofer A;. EMBO J. 2005;24:23-33. (from Pfam)
AIG1 family
Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. [1]. 8742710. Isolation of Arabidopsis genes that differentiate between resistance responses mediated by the RPS2 and RPM1 disease resistance genes. Reuber TL, Ausubel FM;. Plant Cell 1996;8:241-249. (from Pfam)
FeoB small GTPase domain-containing protein
Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions [1]. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent [1]. [1]. 8407793. Characterization of the ferrous iron uptake system of Escherichia coli. Kammler M, Schon C, Hantke K;. J Bacteriol 1993;175:6212-6219. (from Pfam)
GTPase
This HMM identifies the P-loop-containing domain of large numbers of GTPases with ribosome-associated functions, including many involved in ribosome maturation (Der, Era, etc), ribosome rescue (HflX), and protein translation (InfB, Tuf, PrfC).
Ras family
Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See Pfam:PF00009 Pfam:PF00025, Pfam:PF00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices [1]. [1]. 11387043. The Rab GTPase family. Stenmark H, Olkkonen VM;. Genome Biol 2001;2:REVIEWS3007. (from Pfam)
tRNA modification GTPase
tRNA modification GTPase is involved in the modification of the wobble position of certain tRNAs and is one of the G proteins activated by nucleotide-dependent dimerization, such as bacterial MnmE and mitochondrial GTP-binding protein 3
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE
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