Dual-specificity RNA methyltransferase RlmN - Neisseria meningitidis serogroup B (strain M04-240196)

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F0N1E0 (F0N1E0_NEIMO) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 13. History...

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

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

Names and origin

Protein names

Recommended name:
Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849
EC=2.1.1.- HAMAP-Rule MF_01849
EC=2.1.1.192 HAMAP-Rule MF_01849

Alternative name(s):
23S rRNA (adenine(2503)-C(2))-methyltransferase HAMAP-Rule MF_01849
23S rRNA m2A2503 methyltransferase HAMAP-Rule MF_01849
Ribosomal RNA large subunit methyltransferase N HAMAP-Rule MF_01849
tRNA (adenine(37)-C(2))-methyltransferase HAMAP-Rule MF_01849
tRNA m2A37 methyltransferase HAMAP-Rule MF_01849

Gene names

Name:	rlmN HAMAP-Rule MF_01849
Ordered Locus Names:	NMBM04240196_0894 EMBL ADZ01371.1

Organism

Neisseria meningitidis serogroup B (strain M04-240196) [Complete proteome] [HAMAP]

Taxonomic identifier

935593 [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 SAAS SAAS004383 2 S-adenosyl-L-methionine + adenine₃₇ in tRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine₃₇ in tRNA. HAMAP-Rule MF_01849 SAAS SAAS004383
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity. HAMAP-Rule MF_01849 SAAS SAAS004383
Subcellular location	Cytoplasm By similarity 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. HAMAP-Rule MF_01849

Ontologies

Keywords
Biological process	rRNA processing HAMAP-Rule MF_01849 SAAS SAAS004383 tRNA processing HAMAP-Rule MF_01849 SAAS SAAS004383
Cellular component	Cytoplasm HAMAP-Rule MF_01849 SAAS SAAS004383
Ligand	4Fe-4S HAMAP-Rule MF_01849 SAAS SAAS004383 Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine HAMAP-Rule MF_01849 SAAS SAAS004383
Molecular function	Methyltransferase HAMAP-Rule MF_01849 SAAS SAAS004383 Transferase
PTM	Disulfide bond HAMAP-Rule MF_01849 SAAS SAAS004383
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

Regions

Region

164 – 165

S-adenosyl-L-methionine binding By similarity HAMAP-Rule MF_01849

Region

218 – 220

S-adenosyl-L-methionine binding By similarity HAMAP-Rule MF_01849

Sites

Active site

Proton acceptor By similarity HAMAP-Rule MF_01849

Active site

338

S-methylcysteine intermediate By similarity HAMAP-Rule MF_01849

Metal binding

111

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_01849

Metal binding

115

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_01849

Metal binding

118

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_01849

Binding site

196

S-adenosyl-L-methionine By similarity HAMAP-Rule MF_01849

Binding site

295

S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_01849

Amino acid modifications

Disulfide bond

104 ↔ 338

(transient) By similarity HAMAP-Rule MF_01849

Sequences

Sequence

Length

Mass (Da)

Tools

F0N1E0 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: C7810D132143A656
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FASTA

364

40,962

        10         20         30         40         50         60 
MKTNLLNYDL QGLTRHFADM GEKPFRAKQV MRWMHQSGAQ NFDEMTDLAK 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

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References

[1]

"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination."
Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.
Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M04-240196 EMBL ADZ01371.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002423 Genomic DNA. Translation: ADZ01371.1.
RefSeq	YP_005897610.1. NC_017515.1.
3D structure databases
ProteinModelPortal	F0N1E0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADZ01371; ADZ01371; NMBM04240196_0894.
GeneID	12487956.
KEGG	nmq:NMBM04240196_0894.
PATRIC	47168654. VBINeiMen179694_1224.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K06941.
Enzyme and pathway databases
BioCyc	NMEN935593:GLHT-893-MONOMER.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01849. RNA_methyltr_RlmN.
InterPro	IPR013785. Aldolase_TIM. IPR027492. RNA_MTrfase_RlmN. IPR004383. rRNA_lsu_MTrfase_RlmN/Cfr. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR30544. PTHR30544. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF006004. CHP00048. 1 hit.
TIGRFAMs	TIGR00048. TIGR00048. 1 hit.
ProtoNet	Search...

Entry information

Entry name

F0N1E0_NEIMO

Accession

Primary (citable) accession number: F0N1E0

Entry history

Integrated into UniProtKB/TrEMBL:	May 3, 2011
Last sequence update:	May 3, 2011
Last modified:	May 29, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information