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B1XXL6 (RLMN_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Lcho_2871
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesLeptothrix

Protein attributes

Sequence length393 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 – 393393Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849
PRO_0000350237

Regions

Region179 – 1802S-adenosyl-L-methionine binding By similarity
Region233 – 2353S-adenosyl-L-methionine binding By similarity

Sites

Active site921Proton acceptor Potential
Active site3591S-methylcysteine intermediate By similarity
Metal binding1121Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1161Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1191Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site2111S-adenosyl-L-methionine By similarity
Binding site3161S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond105 ↔ 359(transient) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XXL6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 34A9397DB5B1FA23

FASTA39342,738
        10         20         30         40         50         60 
MTAVNLLDFD LDALAAYCEQ LGEKRFRAVQ LFRWIHQRGA ADFGQMSDLA KSLRSKLADV 

        70         80         90        100        110        120 
ACIAPLRVLS EHRSSDGTIK WLFDVGDGNA VETVYIPEDD RATLCISSQA GCAVGCRFCS 

       130        140        150        160        170        180 
TGHQGFSRNL STAEILAQLW YAEHSLRRER AEGVSVGARA ATGPASERII SNVVMMGMGE 

       190        200        210        220        230        240 
PLQNYAAVLP ALRVMLDDHG YGLSRRRVTV STSGVVPMID RLAADLPVAL AVSLHACDDA 

       250        260        270        280        290        300 
LRDVLVPLNR KYPLAELLGA CQAYLASAPR DFITFEYCML DGVNDSDEQA RALLKLVGDK 

       310        320        330        340        350        360 
GPVGRLPCKF NLIPFNPFPE SGLKRSGNER VQAFAQVLID GGLVTTVRKT RGDDIDAACG 

       370        380        390 
QLAGEVQDRT RVQERMTRSP IRVIRSAAQP DAA 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB35136.1.
RefSeqYP_001791901.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1XXL6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395495.Lcho_2871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB35136; ACB35136; Lcho_2871.
GeneID6159746.
KEGGlch:Lcho_2871.
PATRIC22396153. VBILepCho83238_2902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0820.
HOGENOMHOG000217992.
KOK06941.
OMAHEGSKFE.
OrthoDBEOG6DJZ2N.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-2918-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01849. RNA_methyltr_RlmN.
InterProIPR013785. Aldolase_TIM.
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.
TIGRFAMsTIGR00048. TIGR00048. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRLMN_LEPCP
AccessionPrimary (citable) accession number: B1XXL6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 44 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