{'fraction_non_alphanumeric': 0.027977044476327116, 'fraction_numerical': 0.03156384505021521, 'mean_word_length': 5.771844660194175, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Phylogenomic analysis of 16S rRNA:(guanine‐N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino‐methyltransferases

ABSTRACT The sequences of known Escherichia coli 16S rRNA:m2G1207 methyltransferase (MTase) RsmC and hypothetical 16S rRNA:m2G966 MTase encoded by the ygjo open reading frame were used to carry out a database search of other putative m2G‐generating enzymes in finished and unfinished genomic sequences. Sequence comparison and phy‐logenetic analysis of 21 close homologs of RsmC and YgjO revealed the presence of the third paralogous lineage in E. coli and other γ‐Proteobacteria, which might correspond to the subfamily of MTases spe¬cific for G1516 in 16S rRNA. In addition, the com¬parative sequence analysis supported by sequence/ structure threading suggests that rRNA:m2G MTases are very closely related to RNA and DNA:m6A MTases and that these two enzyme families share common architecture of the active site and presum‐ably a similar mechanism of methyl group transfer onto the exocyclic amino group of their target bases.—Bujnicki, J. M. Phylogenomic analysis of 16S rRNA:(guanine‐N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino‐methyltransferases. FASEB J. 14, 2365‐2368 (2000)