Dual-specificity RNA methyltransferase RlmN - Photorhabdus luminescens subsp. laumondii (strain TT01)

Contribute

Send feedback

Read comments (?) or add your own

Q7N709 (RLMN_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. History...

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

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

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:	plu1373

Organism

Photorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]

Taxonomic identifier

243265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus ›

Protein attributes

Sequence length	392 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 – 392

392

Dual-specificity RNA methyltransferase RlmN HAMAP-Rule MF_01849

PRO_0000350307

Regions

Region

187 – 188

S-adenosyl-L-methionine binding By similarity

Region

241 – 243

S-adenosyl-L-methionine binding By similarity

Sites

Active site

113

Proton acceptor Potential

Active site

363

S-methylcysteine intermediate By similarity

Metal binding

133

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

Metal binding

137

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

Metal binding

140

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

Binding site

219

S-adenosyl-L-methionine By similarity

Binding site

320

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

Amino acid modifications

Disulfide bond

126 ↔ 363

(transient) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7N709 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 518BFC5DD9E8D908
Show »

FASTA

392

43,893

        10         20         30         40         50         60 
MSQPNTAAQF AASVVSETPE KKGGKINLLD LNRKQMRQFF IDMGEKPFRA DQVMKWIYHY 

        70         80         90        100        110        120 
CYDDFEQMTD INKILRAKLQ QVAEIRAPEV AEEQRSADGT IKWAITVGDQ QVETVYIPED 

       130        140        150        160        170        180 
DRATLCVSSQ VGCALECKFC STAQQGFNRN LRVSEIIGQV WRAAKIIGSL KSSGRRPITN 

       190        200        210        220        230        240 
VVMMGMGEPL LNLNNVVPAM EIMMDDFGFG LSKRRVTLST SGVVPALDKL GDMIDVALAI 

       250        260        270        280        290        300 
SLHAPTDDVR DDIVPINRKY NIEQFLAGVR RYLTKSNANQ GRVTVEYVML DHINDSVEQA 

       310        320        330        340        350        360 
HQLAECLKET PSKINLIPWN PFPGAPYGRS SNSRIDRFAK VLMEYGFTTI VRKTRGDDID 

       370        380        390 
AACGQLAGDV IDRTKRTLKK RQAGEPIQIR SV

« Hide

References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens."
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K.

Kunst F.
Nat. Biotechnol. 21:1307-1313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TT01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571863 Genomic DNA. Translation: CAE13666.1.
RefSeq	NP_928673.1. NC_005126.1.
3D structure databases
ProteinModelPortal	Q7N709.
ModBase	Search...
Protein-protein interaction databases
STRING	243265.plu1373.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE13666; CAE13666; plu1373.
GeneID	2801351.
KEGG	plu:plu1373.
PATRIC	20506525. VBIPhoLum48522_1521.
Organism-specific databases
GenoList	plu1373.
CMR	Search...
Phylogenomic databases
eggNOG	COG0820.
HOGENOM	HOG000217992.
KO	K06941.
OMA	IYHFGVS.
ProtClustDB	PRK11194.
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_PHOLL

Accession

Primary (citable) accession number: Q7N709

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 70 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

Family and domain databases

Entry information

Relevant documents