CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
33QQMREFFKDLGEKPFacetylation[1]
38FFKDLGEKPFRADQVacetylation[1]
382QGEAIDIKAV*****acetylation[1]
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. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR006638; Elp3/MiaB/NifB.
 IPR027492; RNA_MTrfase_RlmN.
 IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
 IPR007197; rSAM. 
Pfam
 PF04055; Radical_SAM 
SMART
 SM00729; Elp3 
PROSITE
  
PRINTS