Dual-specificity RNA methyltransferase RlmN - Haemophilus influenzae (strain 86-028NP)

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Q4QNH7 (RLMN_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	NTHI0485

Organism

Haemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]

Taxonomic identifier

281310 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Inferred 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. HAMAP-Rule MF_01849
Sequence similarities	Belongs to the radical SAM superfamily. RlmN family.

Ontologies

Keywords
Biological process	rRNA processing tRNA processing
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	rRNA base methylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW rRNA (adenine-C2-)-methyltransferase activity Inferred from electronic annotation. Source: HAMAP rRNA binding Inferred from electronic annotation. Source: HAMAP tRNA (adenine-C2-)-methyltransferase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 390

390

Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849

PRO_0000350202

Regions

Region

184 – 185

S-adenosyl-L-methionine binding By similarity

Region

238 – 240

S-adenosyl-L-methionine binding By similarity

Sites

Active site

110

Proton acceptor Potential

Active site

360

S-methylcysteine intermediate By similarity

Metal binding

130

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

134

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

137

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Binding site

216

S-adenosyl-L-methionine By similarity

Binding site

317

S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond

123 ↔ 360

(transient) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q4QNH7 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: BC2C42F6B6699EFD
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FASTA

390

43,553

        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 NVSNANHGKV TIEYVMLDHV NDGIEHAHQL 

       310        320        330        340        350        360 
AEVLKNTPCK INLIPWNPFP EAPYAKSSNT RIDRFQKTLM EYGFTVIIRK TRGDDIDAAC 

       370        380        390 
GQLAGDVIDR TKRTAMKRQF GQNIGVTEVN

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References

[1]

"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000057 Genomic DNA. Translation: AAX87420.1.
RefSeq	YP_248080.1. NC_007146.2.
3D structure databases
ProteinModelPortal	Q4QNH7.
ModBase	Search...
Protein-protein interaction databases
STRING	281310.NTHI0485.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX87420; AAX87420; NTHI0485.
GeneID	3429802.
KEGG	hit:NTHI0485.
PATRIC	20181139. VBIHaeInf100748_0446.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0820.
HOGENOM	HOG000217992.
KO	K06941.
OMA	MACDFCA.
ProtClustDB	PRK11194.
Enzyme and pathway databases
BioCyc	HINF281310:GJ89-454-MONOMER.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01849. RNA_methyltr_RlmN.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR004383. rRNA_lsu_MTrfase_RlmN. IPR007197. rSAM. [Graphical view]
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF006004. CHP00048. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00048. TIGR00048. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RLMN_HAEI8

Accession

Primary (citable) accession number: Q4QNH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents