Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

Combined Automated Annotation using Multiple IEA Methods

Interaction network containing conserved and essential protein complexes in Escherichia coli.

The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA.

Protein abundance profiling of the Escherichia coli cytosol.

RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA.

The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy.

The binary protein-protein interaction landscape of Escherichia coli.

Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation.

A radically different mechanism for S-adenosylmethionine-dependent methyltransferases.

Structural basis for methyl transfer by a radical SAM enzyme.

Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN.

Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.

Determinants of tRNA Recognition by the Radical SAM Enzyme RlmN.

Distinction between the Cfr methyltransferase conferring antibiotic resistance and the housekeeping RlmN methyltransferase.

RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift.

UniProt entry P36979 (RLMN_ECOLI)