Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
16S rRNA methyltransferase RsmB/F
This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme [1,2]. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA [1,2]. [1]. 14997580. Crystal structure of human p120 homologue protein PH1374 from Pyrococcus horikoshii. Ishikawa I, Sakai N, Tamura T, Yao M, Watanabe N, Tanaka I;. Proteins. 2004;54:814-816. [2]. 20558545. Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus. Demirci H, Larsen LH, Hansen T, Rasmussen A, Cadambi A, Gregory ST, Kirpekar F, Jogl G;. RNA. 2010;16:1584-1596. (from Pfam)
transcription antitermination factor NusB
The NusB protein is involved in the regulation of rRNA biosynthesis by transcriptional antitermination. NMR structure. [1]. 9670024. Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein. Huenges M, Rolz C, Gschwind R, Peteranderl R, Berglechner F, Richter G, Bacher A, Kessler H,Gemmecker G;. EMBO J 1998;17:4092-4100. (from Pfam)
RsmB/NOP family class I SAM-dependent RNA methyltransferase
RsmB/NOP family class I SAM-dependent RNA methyltransferase similar to tRNA (cytosine(34)-C(5))-methyltransferase, which methylates cytosine at specific positions of intron-containing tRNA(Leu)(CAA) precursors and tRNA(Gly)(GCC) precursors
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on