Tag | Content |
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CPLM ID | CPLM-006696 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dual-specificity RNA methyltransferase RlmN |
Protein Synonyms/Alias | 23S rRNA (adenine(2503)-C(2))-methyltransferase; 23S rRNA m2A2503 methyltransferase; Ribosomal RNA large subunit methyltransferase N; tRNA (adenine(37)-C(2))-methyltransferase; tRNA m2A37 methyltransferase |
Gene Name | rlmN |
Gene Synonyms/Alias | yfgB; b2517; JW2501 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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33 | QQMREFFKDLGEKPF | acetylation | [1] | 38 | FFKDLGEKPFRADQV | acetylation | [1] | 382 | QGEAIDIKAV***** | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. |
Sequence Annotation | REGION 179 180 S-adenosyl-L-methionine binding. REGION 233 235 S-adenosyl-L-methionine binding. ACT_SITE 105 105 Proton acceptor (Potential). ACT_SITE 355 355 S-methylcysteine intermediate. METAL 125 125 Iron-sulfur (4Fe-4S-S-AdoMet). METAL 129 129 Iron-sulfur (4Fe-4S-S-AdoMet). METAL 132 132 Iron-sulfur (4Fe-4S-S-AdoMet). BINDING 211 211 S-adenosyl-L-methionine. BINDING 312 312 S-adenosyl-L-methionine; via amide DISULFID 118 355 (transient) (Probable). |
Keyword | 3D-structure; 4Fe-4S; Antibiotic resistance; Complete proteome; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 384 AA |
Protein Sequence | MSEQLVTPEN VTTKDGKINL LDLNRQQMRE FFKDLGEKPF RADQVMKWMY HYCCDNFDEM 60 TDINKVLRGK LKEVAEIRAP EVVEEQRSSD GTIKWAIAVG DQRVETVYIP EDDRATLCVS 120 SQVGCALECK FCSTAQQGFN RNLRVSEIIG QVWRAAKIVG AAKVTGQRPI TNVVMMGMGE 180 PLLNLNNVVP AMEIMLDDFG FGLSKRRVTL STSGVVPALD KLGDMIDVAL AISLHAPNDE 240 IRDEIVPINK KYNIETFLAA VRRYLEKSNA NQGRVTIEYV MLDHVNDGTE HAHQLAELLK 300 DTPCKINLIP WNPFPGAPYG RSSNSRIDRF SKVLMSYGFT TIVRKTRGDD IDAACGQLAG 360 DVIDRTKRTL RKRMQGEAID IKAV 384 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IDA:EcoCyc. GO:0019843; F:rRNA binding; IEA:HAMAP. GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IDA:UniProtKB. GO:0000049; F:tRNA binding; IDA:UniProtKB. GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. GO:0070475; P:rRNA base methylation; IMP:EcoCyc. |
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