Full name: |
Ribosomal RNA small subunit methyltransferase J |
Synonym: |
YhiQ |
GI: |
388479744 |
Orf: |
|
COG: |
COG0742 |
UniProt: |
P68567 |
Structures: |
|
2PGX |
|
Complex: |
|
Enzyme type: |
methyltransferase |
Position of modification - modification: |
s:1516(1516) - m2G
|
Comments:
RsmJ catalyzes formation of m2G1516 in the loop of hairpin 45 at the 3’-end of 16S ribosomal RNA. Recombinant RsmJ specifically methylates 30S subunits extracted from the deletion strain. All ribosomal guanine-(N2)-methyltransferases have similar AdoMet-binding sites. Moreover, comparative sequence analysis supported by sequence/structure threading suggests that rRNA:m2G MTases are very closely related to RNA and DNA:m6A MTases and that these two enzyme families share common architecture of the active site and presumably a similar mechanism of methyl group transfer onto the exocyclic amino group of their target bases.
Protein sequence:
MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAGLG
RDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDA
DGLLEPARLLATKRVVVKRPDYAPPLANVATPNAVVTKGHRFDIYAGTPV
Enzymatic activities:
Reaction
| Substrate
| Type
| Position
|
G:m2G
|
rRNA (r) |
SSU/16S/prokaryotic cytosol |
1516 |
Publications:
Title |
Authors |
Journal |
Details |
PubMed Id |
DOI |
Phylogenomic analysis of 16S rRNA:(guanine-N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino-methyltransferases. |
Bujnicki JM |
FASEB J |
[details]
|
11053259
|
-
|
Ribosomal RNA guanine-(N2)-methyltransferases and their targets. |
Sergiev PV, Bogdanov AA, Dontsova OA |
Nucleic Acids Res |
[details]
|
17389639
|
-
|
YhiQ Is RsmJ, the Methyltransferase Responsible for Methylation of G1516 in 16S rRNA of E. coli. |
Basturea GN, Dague DR, Deutscher MP, Rudd KE |
J Mol Biol |
[details]
|
22079366
|
-
|
Copyright © Genesilico - All rights reserved
If you have any advice or suggestions for corrections or improvements, please contact:
Andrea Cappannini - lp.vog.bcmii@ininnappaca