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O67680 (RSMA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal RNA small subunit methyltransferase A

EC=2.1.1.182
Alternative name(s):
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase
16S rRNA dimethyladenosine transferase
16S rRNA dimethylase
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Gene names
Name:rsmA
Synonyms:ksgA
Ordered Locus Names:aq_1816
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits By similarity. HAMAP-Rule MF_00607

Catalytic activity

4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)-dimethyladenine(1519) in 16S rRNA. HAMAP-Rule MF_00607

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00607.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Ribosomal RNA small subunit methyltransferase A HAMAP-Rule MF_00607
PRO_0000101474

Sites

Binding site111S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site131S-adenosyl-L-methionine; via amide nitrogen
Binding site381S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site601S-adenosyl-L-methionine
Binding site831S-adenosyl-L-methionine
Binding site1011S-adenosyl-L-methionine
Site1051Interaction with RNA
Site1981Interaction with RNA
Site2021Interaction with RNA
Site2041Interaction with RNA

Secondary structure

................................................. 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67680 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 259FA7AA81786AF8

FASTA24828,355
        10         20         30         40         50         60 
MVRLKKSFGQ HLLVSEGVLK KIAEELNIEE GNTVVEVGGG TGNLTKVLLQ HPLKKLYVIE 

        70         80         90        100        110        120 
LDREMVENLK SIGDERLEVI NEDASKFPFC SLGKELKVVG NLPYNVASLI IENTVYNKDC 

       130        140        150        160        170        180 
VPLAVFMVQK EVAEKLQGKK DTGWLSVFVR TFYDVNYVMT VPPRFFVPPP KVQSAVIKLV 

       190        200        210        220        230        240 
KNEKFPVKDL KNYKKFLTKI FQNRRKVLRK KIPEELLKEA GINPDARVEQ LSLEDFFKLY 


RLIEDSGE 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Structural basis for binding of RNA and cofactor by a KsgA methyltransferase."
Tu C., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., Ji X.
Structure 17:374-385(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEXES WITH RNA AND S-ADENOSYL-L-HOMOCYSTEINE, RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07637.1.
PIRF70456.
RefSeqNP_214246.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FTCX-ray1.68A1-248[»]
3FTDX-ray1.44A1-248[»]
3FTEX-ray3.00A1-248[»]
3FTFX-ray2.80A1-248[»]
3R9XX-ray2.80B1-248[»]
ProteinModelPortalO67680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07637; AAC07637; aq_1816.
GeneID1193487.
KEGGaae:aq_1816.
PATRIC20960604. VBIAquAeo85532_1403.

Phylogenomic databases

eggNOGCOG0030.
HOGENOMHOG000227962.
KOK02528.
OMAITSEILF.
OrthoDBEOG66F08Z.
ProtClustDBPRK00274.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1301-MONOMER.

Family and domain databases

Gene3D1.10.8.100. 1 hit.
HAMAPMF_00607. 16SrRNA_methyltr_A.
InterProIPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR001737. rRNA_Ade_methylase_transferase.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
[Graphical view]
PANTHERPTHR11727. PTHR11727. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTSM00650. rADc. 1 hit.
[Graphical view]
TIGRFAMsTIGR00755. ksgA. 1 hit.
PROSITEPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO67680.

Entry information

Entry nameRSMA_AQUAE
AccessionPrimary (citable) accession number: O67680
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references