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A5UAC2 (RLMN_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:CGSHiEE_01185
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length390 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 caution

The sequence ABQ97723.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849
PRO_0000350203

Regions

Region184 – 1852S-adenosyl-L-methionine binding By similarity
Region238 – 2403S-adenosyl-L-methionine binding By similarity

Sites

Active site1101Proton acceptor Potential
Active site3601S-methylcysteine intermediate By similarity
Metal binding1301Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1341Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1371Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site2161S-adenosyl-L-methionine By similarity
Binding site3171S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond123 ↔ 360(transient) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UAC2 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 85E174CE9CF12465

FASTA39043,570
        10         20         30         40         50         60 
MCNNEAKMSE LLSVQSDAPA KKINLMDLTR QQMREFFKEL GEKPFRADQL VKWIYHFGED 

        70         80         90        100        110        120 
NFDNMTNINK KLREKLKAVA EIKAPEVAVE QRSADGTIKW AMQVGEQQVE TVYIPEADRA 

       130        140        150        160        170        180 
TLCVSSQVGC ALACTFCSTA QQGFNRNLTV SEIIGQVWRA SKIIGNFGVT GVRPITNVVM 

       190        200        210        220        230        240 
MGMGEPLLNV ANVVPAMEIM LDDFAYGLSK RRVTLSTSGV VPALDNLSKM IDVALAISLH 

       250        260        270        280        290        300 
APNDELRDEI VPINKKYNIK TLIDSVNRYL TVSNANHGKV TIEYVMLDHV NDGVEHAHQL 

       310        320        330        340        350        360 
ADVLKNTPCK INLIPWNPFP EAPYAKSSNT RIDRFQKTLM EYDFTVIIRK TRGDDIDAAC 

       370        380        390 
GQLAGDVIDR TKRTAMKRQF GQNIGVTEVN 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ97723.1. Different initiation.
RefSeqYP_001290106.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UAC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_01185.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ97723; ABQ97723; CGSHiEE_01185.
GeneID5224754.
KEGGhip:CGSHiEE_01185.
PATRIC20276473. VBIHaeInf81350_0235.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0820.
HOGENOMHOG000217992.
KOK06941.
OrthoDBEOG6DJZ2N.
ProtClustDBPRK11194.

Enzyme and pathway databases

BioCycHINF374930:GJDD-223-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_HAEIE
AccessionPrimary (citable) accession number: A5UAC2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 45 of the entry and version 2 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