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Q9LCY2 (RSMG_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribosomal RNA small subunit methyltransferase G
EC=2.1.1.170
Alternative name(s):
16S rRNA 7-methylguanosine methyltransferase
Short name=16S rRNA m7G methyltransferase
Glucose-inhibited division protein B
Gene names
Name:rsmG
Synonyms:gidB
Ordered Locus Names:TTHA1971
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate. Ref.3

Catalytic activity

S-adenosyl-L-methionine + guanine(527) in 16S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(527) in 16S rRNA. HAMAP-Rule MF_00074

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00074.

Disruption phenotype

Low-level streptomycin resistance. Ref.3

Sequence similarities

Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.

Sequence caution

The sequence CAB89206.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA (guanine-N7)-methylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionrRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Ribosomal RNA small subunit methyltransferase G HAMAP-Rule MF_00074
PRO_0000184358

Regions

Region111 – 1133S-adenosyl-L-methionine binding HAMAP-Rule MF_00074
Region139 – 1402S-adenosyl-L-methionine binding HAMAP-Rule MF_00074
Region245 – 2462RNA binding Potential

Sites

Binding site881S-adenosyl-L-methionine; via carbonyl oxygen
Binding site931S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1581S-adenosyl-L-methionine

Amino acid modifications

Disulfide bond164 ↔ 249 Ref.3

Experimental info

Sequence conflict198 – 22124ALERL…SGEAR → LWSGSAGGLGRSSPSKLPSP GRRC in CAB89206. Ref.1
Sequence conflict2291T → R in CAB89206. Ref.1

Secondary structure

1 ............................................ 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9LCY2 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: D346C3401D4A1619

FASTA24926,832
        10         20         30         40         50         60 
MFHGKHPGGL SERGRALLLE GGKALGLDLK PHLEAFSRLY ALLQEASGKV NLTALRGEEE 

        70         80         90        100        110        120 
VVVKHFLDSL TLLRLPLWQG PLRVLDLGTG AGFPGLPLKI VRPELELVLV DATRKKVAFV 

       130        140        150        160        170        180 
ERAIEVLGLK GARALWGRAE VLAREAGHRE AYARAVARAV APLCVLSELL LPFLEVGGAA 

       190        200        210        220        230        240 
VAMKGPRVEE ELAPLPPALE RLGGRLGEVL ALQLPLSGEA RHLVVLEKTA PTPPAYPRRP 


GVPERHPLC

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of the dnaA upstream region of Thermus thermophilus."
Nardmann J., Messer W.
Gene 261:299-303(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG."
Gregory S.T., Demirci H., Belardinelli R., Monshupanee T., Gualerzi C., Dahlberg A.E., Jogl G.
RNA 15:1693-1704(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH AMP; S-ADENOSYL-L-HOMOCYSTEINE AND S-ADENOSYL-L-METHIONINE, FUNCTION, DISRUPTION PHENOTYPE, DISULFIDE BOND.
Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ277593 Genomic DNA. Translation: CAB89206.1. Different initiation.
AP008226 Genomic DNA. Translation: BAD71794.1.
RefSeqYP_145237.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3G88X-ray1.87A/B1-249[»]
3G89X-ray1.50A/B1-249[»]
3G8AX-ray2.10A/B/C/D/E/F1-249[»]
3G8BX-ray2.10A/B1-249[»]
ProteinModelPortalQ9LCY2.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA1971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71794; BAD71794; BAD71794.
GeneID3169844.
KEGGttj:TTHA1971.
PATRIC23958921. VBITheThe93045_1942.

Phylogenomic databases

eggNOGCOG0357.
HOGENOMHOG000221014.
KOK03501.
OMAAITHPNS.
ProtClustDBPRK00107.

Family and domain databases

HAMAPMF_00074. 16SrRNA_methyltr_G.
InterProIPR003682. rRNA_ssu_MeTfrase_G.
[Graphical view]
PfamPF02527. GidB. 1 hit.
[Graphical view]
PIRSFPIRSF003078. GidB. 1 hit.
TIGRFAMsTIGR00138. gidB. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9LCY2.

Entry information

Entry nameRSMG_THET8
AccessionPrimary (citable) accession number: Q9LCY2
Secondary accession number(s): Q5SGV9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: March 29, 2005
Last modified: May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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