2.1.1.183: 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
This is an abbreviated version!
For detailed information about 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.183
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2.1.1.183
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pombe
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schizosaccharomyces
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tri-snrnps
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mitosis
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pre-rrnas
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nucleolar
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fission
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collagen
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ribonucleoprotein
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oncogene
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spindle
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thioredoxin-like
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pre-ribosomal
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anaphase-promoting
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metastasis-associated
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salivary
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pirin
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spliceosomal
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transketolase
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v-ha-ras
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adenoid
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cyclosome
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snrnp
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cystic
- 2.1.1.183
- pombe
-
schizosaccharomyces
-
tri-snrnps
-
mitosis
- pre-rrnas
-
nucleolar
-
fission
- collagen
- ribonucleoprotein
- oncogene
-
spindle
-
thioredoxin-like
-
pre-ribosomal
-
anaphase-promoting
-
metastasis-associated
-
salivary
- pirin
-
spliceosomal
- transketolase
-
v-ha-ras
-
adenoid
-
cyclosome
-
snrnp
-
cystic
Reaction
4 S-adenosyl-L-methionine + = 4 S-adenosyl-L-homocysteine +
Synonyms
18S rRNA dimethylase Dim1p, DIM1, Dim1p, EC 2.1.1.48, KIDIM1, m2(6)A dimethylase, ScDim1
ECTree
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Engineering
Engineering on EC 2.1.1.183 - 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
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E85A
the altered protein is able to complement for Dim1 but yields a protein with no catalytic activity as determined by primer extension of 18S rRNA. The expected primer extension stops at 1779 and 1780 are missing in rRNA extracted from the strain expressing catalytically inactive ScDim1. The single mutant shows no change in growth rate of yeast at 18, 25, 30, and 37°C
additional information
to delineate regions of the eukaryotic Dim1 critical to its function, KsgA/Dim1 chimeras are created and tested. Construction of six chimeras that result from swapping the two domains of Saccharomyces cerevisiae Dim1, Escherichia coli KsgA, and Methanocaldococcus jannaschii Dim1. Of the chimeras, only one constructed with the N-terminal domain from eukaryotic Dim1 and the C-terminal domain from archaeal Dim1 is able to complement for the eukaryotic Dim1, suggesting that eukaryotic-specific Dim1 function resides in the N-terminal domain, where few structural differences are observed between members of the KsgA/Dim1 family