Dual-specificity RNA methyltransferase RlmN - Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18)

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A1KUD6 (RLMN_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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:	NMC1245

Organism

Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP]

Taxonomic identifier

272831 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length	364 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 – 364

364

Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849

PRO_0000350280

Regions

Region

164 – 165

S-adenosyl-L-methionine binding By similarity

Region

218 – 220

S-adenosyl-L-methionine binding By similarity

Sites

Active site

Proton acceptor Potential

Active site

338

S-methylcysteine intermediate By similarity

Metal binding

111

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

Metal binding

115

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

Metal binding

118

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

Binding site

196

S-adenosyl-L-methionine By similarity

Binding site

295

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

Amino acid modifications

Disulfide bond

104 ↔ 338

(transient) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A1KUD6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C2482C9E42CB0F74
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FASTA

364

40,961

        10         20         30         40         50         60 
MKTNLLNYDL QGLTRHFADM GEKPFRAKQV MRWMHQSGAQ NFNEMTDLAK SLRHKLNEQA 

        70         80         90        100        110        120 
GIEIPKLMMS QKSSDGTRKW LLDVGTGNGV ETVFIPESDR GTLCISSQVG CALECTFCST 

       130        140        150        160        170        180 
GRQGFNRNLT AAEIIGQLWW ANKAMGVTPK NERVISNVVM MGMGEPMANF DNVVTALSIM 

       190        200        210        220        230        240 
LDDHGYGLSR RRVTVSTSGM VPQMDRLRDV MPVALAVSLH ASNDEVRNQI VPLNKKYPLK 

       250        260        270        280        290        300 
ELMAACQRYL VKAPRDFITF EYVMLDGIND KAQHARELIE LVKDVPCKFN LIPFNPFPNS 

       310        320        330        340        350        360 
GYERSSNENI RVFRDILQQA GFVVTVRKTR GDDIDAACGQ LAGQVQDKTR RQQKWQQILI 


GQQG

« Hide

References

[1]

"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M.

Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / FAM18.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM421808 Genomic DNA. Translation: CAM10479.1.
RefSeq	YP_975265.1. NC_008767.1.
3D structure databases
ProteinModelPortal	A1KUD6.
ModBase	Search...
Protein-protein interaction databases
STRING	272831.NMC1245.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAM10479; CAM10479; NMC1245.
GeneID	4676238.
KEGG	nmc:NMC1245.
PATRIC	20352496. VBINeiMen17609_1496.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0820.
HOGENOM	HOG000217992.
KO	K06941.
OMA	IYHFGVS.
ProtClustDB	CLSK877994.
Enzyme and pathway databases
BioCyc	NMEN272831:GJDX-1186-MONOMER.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01849. RNA_methyltr_RlmN.
InterPro	IPR013785. Aldolase_TIM. IPR004383. rRNA_lsu_MTrfase_RlmN. IPR007197. rSAM. [Graphical view]
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF006004. CHP00048. 1 hit.
TIGRFAMs	TIGR00048. TIGR00048. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RLMN_NEIMF

Accession

Primary (citable) accession number: A1KUD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 49 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