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A4IY03 (RLMN_FRATW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dual-specificity RNA methyltransferase RlmN

EC=2.1.1.-
EC=2.1.1.192
Alternative name(s):
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 names
Name:rlmN
Ordered Locus Names:FTW_0968
OrganismFrancisella tularensis subsp. tularensis (strain WY96-3418) [Complete proteome] [HAMAP]
Taxonomic identifier418136 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01849

Catalytic activity

2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA. HAMAP-Rule MF_01849

2 S-adenosyl-L-methionine + adenine37 in tRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA. HAMAP-Rule MF_01849

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01849.

Miscellaneous

Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue By similarity.

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849
PRO_0000350187

Regions

Region167 – 1682S-adenosyl-L-methionine binding By similarity
Region221 – 2233S-adenosyl-L-methionine binding By similarity

Sites

Active site931Proton acceptor Potential
Active site3431S-methylcysteine intermediate By similarity
Metal binding1131Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1171Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1201Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site1991S-adenosyl-L-methionine By similarity
Binding site3001S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond106 ↔ 343(transient) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IY03 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 4988A14166735EC7

FASTA37041,478
        10         20         30         40         50         60 
MQQDKVNLLG LNQKAIEDFF ISIGEKKFHA RQVFKWIHKK GVIDFDAMTD LGKNLRHKLK 

        70         80         90        100        110        120 
EKAQITIPKV VFSKASKDGT HKWLIDVGGS AVETVFILEE GRGTLCVSSQ VGCTLNCSFC 

       130        140        150        160        170        180 
STGKQGFNRN LSAAEVIAQL WIAARTLSKT DGEHDFTVTN IVMMGMGEPL MNFENVVPAM 

       190        200        210        220        230        240 
DIMMDDLAYG LSRRKVTLST SGVVPRIYDL LEQSGVSLAV SLHAPNDMLR NEIVPINKKY 

       250        260        270        280        290        300 
NIDELLEACK LYAQKGPHKH ITFEYTLMEE VNDNLSDAEE LVALLKSREV PAKINLIPFN 

       310        320        330        340        350        360 
PYPGTPYKKP SNNRIHRFKE FLQHNGFVTT VRKTRGDDID AACGQLAGDV MDKTNRKQRY 

       370 
LKKLGDTNAN 

« Hide

References

[1]"Complete genomic characterization of a pathogenic A.II strain of Francisella tularensis subspecies tularensis."
Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., Wagner D.M., Brettin T.S. expand/collapse author list , Brown N., Gilna P., Keim P.S.
PLoS ONE 2:E947-E947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WY96-3418.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000608 Genomic DNA. Translation: ABO46804.1.
RefSeqYP_001121925.1. NC_009257.1.

3D structure databases

ProteinModelPortalA4IY03.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418136.FTW_0968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO46804; ABO46804; FTW_0968.
GeneID4959792.
KEGGftw:FTW_0968.
PATRIC17969376. VBIFraTul58433_1000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0820.
HOGENOMHOG000217992.
KOK06941.
OMAIYHFGVS.
OrthoDBEOG6DJZ2N.
ProtClustDBCLSK934825.

Enzyme and pathway databases

BioCycFTUL418136:GHXJ-916-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01849. RNA_methyltr_RlmN.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR027492. RNA_MTrfase_RlmN.
IPR004383. rRNA_lsu_MTrfase_RlmN/Cfr.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR30544. PTHR30544. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF006004. CHP00048. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00048. TIGR00048. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRLMN_FRATW
AccessionPrimary (citable) accession number: A4IY03
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families