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Q732K6 (RLMN_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:
Probable 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:BCE_3906
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length362 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 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 – 362362Probable dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849
PRO_0000350028

Regions

Region175 – 1762S-adenosyl-L-methionine binding By similarity
Region230 – 2323S-adenosyl-L-methionine binding By similarity

Sites

Active site1051Proton acceptor Potential
Active site3491S-methylcysteine intermediate By similarity
Metal binding1251Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1291Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1321Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site2071S-adenosyl-L-methionine By similarity
Binding site3061S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond118 ↔ 349(transient) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q732K6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5D1D0D3E937245BD

FASTA36241,553
        10         20         30         40         50         60 
METTVRKQKK NLETKKPSIY SLQLHEMQDW LKEQGEPKFR AGQIFDWLYK KRVKNYEDMS 

        70         80         90        100        110        120 
NLSKGLREKL SNSFDITTLN TLVKQTSSDG TIKFLFQLYD GYSIETVLMR HEYGNSICVT 

       130        140        150        160        170        180 
TQVGCRIGCT FCASTLGGLK RNLEAGEIVA QVVEVQRALD ESEERVSSLV VMGIGEPFDN 

       190        200        210        220        230        240 
YDNLMGFLRI INHEKGLHIG ARHMTVSTSG IIPKIYKFAE EDLQINFAIS LHAPNSELRS 

       250        260        270        280        290        300 
KLMPINRAYK LPDLMEAIKY YVNRTGRRIT FEYGLFGGEN DQVEHAEELA ALLKGVKCHV 

       310        320        330        340        350        360 
NLIPVNYVPE RDYVRTPREQ IFLFEKTLKD RGVNVTIRRE QGHDIDAACG QLRAKERKEE 


TR 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS42811.1.
RefSeqNP_980203.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ732K6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_3906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS42811; AAS42811; BCE_3906.
GeneID2748697.
KEGGbca:BCE_3906.
PATRIC18856468. VBIBacCer118379_3733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0820.
HOGENOMHOG000217991.
KOK06941.
OMACVSCQIG.
OrthoDBEOG6DJZ2N.
ProtClustDBPRK14455.

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_BACC1
AccessionPrimary (citable) accession number: Q732K6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 71 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