ID Card:
| Full name: |
Chloroplast MraW-Like |
| GI: |
1063731170
|
| Enzyme type: |
methyltransferase |
Protein sequence:
MAGVIRAKQLFLCSSILSSNNNKVLSRLPRRSINVIAGNLNSSETKKKEKEKRKRRKEIEVEKATAEAVVNKEKRRTRSSRGYELADGDEVPSSHVPVMLGEVLDIFSSVRLRSFVDCTLGAAGHSSSIIQSHSELKNFVGMDVDPVARKLGHFHIDSLMHPTLKASIVLKNFKYIKSVIADTQPELLDVGVDGILMDLGMSSMQVNNPERGFSVLQEGPLDMRMDPQATLTAEDIVNSWPESELGRVLRDYGEESNWYLLQNRIVKARLNGGLHSTGELVDLIRGTSPASRGGRQGWIKTATRVFQGLRIAVNDELKTLQNSLYSSFDVLAPGGRLAVISFHSLEDRVVKQTFLDILGFQREEINGEGSSVKPERQIEERVEKELKEKEEWIKQTVIASKGVILTKRPITPSEEEERLNRRARSAKLRVIQKL
Comments:
Chloropoplast-localized rRNA methyltransferase (Chroloplast Mraw-like) belongs to the mraw methylase protein family and is the Arabidopsis ortholog of bacterial MraW/ RsmH proteins. It is an AdoMet-Mtases, a class of enzymes that uses S-adenosyl-L-methionine (SAM or AdoMt) as a substrate for methyl transfer, thereby generating the S-adenosyl-L-homocysteine. It accounts for the N4-methylation of C1352 in chloroplast 16S rRNA, which is indispensable for the accumulation of chloroplast ribosomes. Noteworthy, loss of CMAL leads to a defect in chloroplast function. Indeed, the loss of this protein brings abnormal A.thaliana morphology, in leaf and root development. This suggests a critical role of CMAL in A.thaliana development and growth.
| Reaction |
Substrate |
SubstrateType |
Position |
(Anti)Codon |
Modified (Anti)Codon |
Amino Acid Change |
Transcript Name |
Transcript Region |
Cellular Localization |
References |
|
C:m4C
|
RNA |
rRNA |
1352 |
|
|
|
16S-SSU |
|
Chloroplast |
32095829
|
Publications:
| Title |
Authors |
Journal |
Details |
PubMed Id |
DOI |
| The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development. |
Meijuan Zou,Ying Mu,Xin Chai,Min Ouyang,Long-Jiang Yu,Lixin Zhang,Jörg Meurer,Wei Chi |
Nucleic Acids Res |
[details]
|
32095829
|
-
|