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Protein

Ribosomal RNA large subunit methyltransferase M

Gene

rlmM

Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + cytidine(2498) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(2498) in 23S rRNA.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei188S-adenosyl-L-methionineUniRule annotation1
Binding sitei240S-adenosyl-L-methionineUniRule annotation1
Binding sitei260S-adenosyl-L-methionineUniRule annotation1
Binding sitei277S-adenosyl-L-methionineUniRule annotation1
Active sitei306Proton acceptorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal RNA large subunit methyltransferase MUniRule annotation (EC:2.1.1.186UniRule annotation)
Alternative name(s):
23S rRNA (cytidine2498-2'-O)-methyltransferaseUniRule annotation
23S rRNA 2'-O-ribose methyltransferase RlmMUniRule annotation
Gene namesi
Name:rlmMUniRule annotation
Ordered Locus Names:ECIAI39_3228
OrganismiEscherichia coli O7:K1 (strain IAI39 / ExPEC)
Taxonomic identifieri585057 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000749 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002015181 – 366Ribosomal RNA large subunit methyltransferase MAdd BLAST366

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7NVV4.
SMRiB7NVV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 224S-adenosyl-L-methionine bindingUniRule annotation4

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. RlmM subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000247137.
KOiK06968.
OMAiVIFECYQ.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01551. 23SrRNA_methyltr_M. 1 hit.
InterProiIPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR011224. rRNA_MeTrfase_M.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
PIRSFiPIRSF028774. UCP028774. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

B7NVV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKVVLLCRP GFEKECAAEI TDKAGQREIF GFARVKENAG YVIYECYQPD
60 70 80 90 100
DGDKLIRELP FSSLIFARQW FVVGELLQHL PPEDRITPIV GMLQGVVEKG
110 120 130 140 150
GELRVEVADT NESKELLKFC RKFTVPLRAA LRDAGVLANY ETPKRPVVHV
160 170 180 190 200
FFIAPGCCYT GYSYSNNNSP FYMGIPRLKF PADAPSRSTL KLEEAFHVFI
210 220 230 240 250
PADEWDERLA NGMWAVDLGA CPGGWTYQLV KRNMWVYSVD NGPMAQSLMD
260 270 280 290 300
TGQVTWLRED GFKFRPTRSN ISWMVCDMVE KPAKVAALMA QWLVNGWCRE
310 320 330 340 350
TIFNLKLPMK KRYEEVSHNL AYIQAQLDEH GINAQIQARQ LYHDREEVTV
360
HVRRIWAAVG GRRDER
Length:366
Mass (Da):41,905
Last modified:March 24, 2009 - v1
Checksum:i595EE105DFB03677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928164 Genomic DNA. Translation: CAR19347.1.
RefSeqiWP_001045520.1. NC_011750.1.
YP_002409152.1. NC_011750.1.

Genome annotation databases

EnsemblBacteriaiCAR19347; CAR19347; ECIAI39_3228.
GeneIDi7151451.
KEGGiect:ECIAI39_3228.
PATRICi18335329. VBIEscCol51957_3354.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928164 Genomic DNA. Translation: CAR19347.1.
RefSeqiWP_001045520.1. NC_011750.1.
YP_002409152.1. NC_011750.1.

3D structure databases

ProteinModelPortaliB7NVV4.
SMRiB7NVV4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR19347; CAR19347; ECIAI39_3228.
GeneIDi7151451.
KEGGiect:ECIAI39_3228.
PATRICi18335329. VBIEscCol51957_3354.

Phylogenomic databases

HOGENOMiHOG000247137.
KOiK06968.
OMAiVIFECYQ.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01551. 23SrRNA_methyltr_M. 1 hit.
InterProiIPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR011224. rRNA_MeTrfase_M.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
PIRSFiPIRSF028774. UCP028774. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRLMM_ECO7I
AccessioniPrimary (citable) accession number: B7NVV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.