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C7BKH3 (C7BKH3_PHOAA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 29. Feed History...

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

Protein namesRecommended name:
Ribosomal RNA small subunit methyltransferase A HAMAP-Rule MF_00607
EC=2.1.1.182 HAMAP-Rule MF_00607
Alternative name(s):
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase HAMAP-Rule MF_00607
16S rRNA dimethyladenosine transferase HAMAP-Rule MF_00607
16S rRNA dimethylase HAMAP-Rule MF_00607
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase HAMAP-Rule MF_00607
Gene names
Name:rsmA HAMAP-Rule MF_00607
Synonyms:ksgA HAMAP-Rule MF_00607 EMBL CAQ82659.1
Ordered Locus Names:PAU_00567 EMBL CAQ82659.1
OrganismPhotorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2)) [Complete proteome] [HAMAP]
Taxonomic identifier553480 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus ›

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 SAAS SAAS023165

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00607.

Sequence similarities

Belongs to the methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily. HAMAP-Rule MF_00607

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site181S-adenosyl-L-methionine; via carbonyl oxygen By similarity HAMAP-Rule MF_00607
Binding site201S-adenosyl-L-methionine; via amide nitrogen By similarity HAMAP-Rule MF_00607
Binding site451S-adenosyl-L-methionine; via carbonyl oxygen By similarity HAMAP-Rule MF_00607
Binding site661S-adenosyl-L-methionine By similarity HAMAP-Rule MF_00607
Binding site911S-adenosyl-L-methionine By similarity HAMAP-Rule MF_00607
Binding site1131S-adenosyl-L-methionine By similarity HAMAP-Rule MF_00607

Sequences

Sequence LengthMass (Da)Tools
C7BKH3 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: F680E56A249674FD

FASTA27230,596
        10         20         30         40         50         60 
MNNRVHQGHF ARKRFGQNFL TDQFVIDSIV AAINPQPGQA VLEIGPGLGA LTEPVGERMD 

        70         80         90        100        110        120 
KMTVVELDRD LAARLQVHPQ LKDKLTIIQQ DAMTVNFGEL SQQRGLPLRV FGNLPYNIST 

       130        140        150        160        170        180 
PLMFHLFSYT DAIADMHFML QKEVVNRLVA GPGSKAFGRL SVMAQYYCQV IPVLEVPPTA 

       190        200        210        220        230        240 
FTPAPKVDSA VVRLIPHKSI PYPVKNIRML SRITTQAFNQ RRKTIRNSLG DLFTVEQLTE 

       250        260        270 
FGIDPSTRAE NISVEQYCKM ANYLSEQPEM QL

« Hide

References

[1]"Comparative genomics of the emerging human pathogen Photorhabdus asymbiotica with the insect pathogen Photorhabdus luminescens."
Wilkinson P., Waterfield N.R., Crossman L., Corton C., Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., Doggett J., Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Arrowsmith C., Churcher C., Harris D. expand/collapse author list , Thompson N.R., Quail M., Parkhill J., Ffrench-Constant R.H.
BMC Genomics 10:302-302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43949 / 3105-77.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM162591 Genomic DNA. Translation: CAQ82659.1.
RefSeqYP_003039404.1. NC_012962.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING291112.PAU_00567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ82659; CAQ82659; PAU_00567.
GeneID13861020.
KEGGpay:PAU_00567.
PATRIC20494723. VBIPhoAsy71438_0651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227962.
KOK02528.
OMAPVPNVDS.
ProtClustDBPRK00274.

Enzyme and pathway databases

BioCycPASY291112:GJQ0-584-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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC7BKH3_PHOAA
AccessionPrimary (citable) accession number: C7BKH3
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info