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Information on EC 2.1.1.206 - tRNA (cytidine56-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.206
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.206 tRNA (cytidine56-2'-O)-methyltransferase
IUBMB Comments
The archaeal enzyme specifically catalyses the S-adenosyl-L-methionine dependent 2′-O-ribose methylation of cytidine at position 56 in tRNA transcripts.
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
- 2.1.1.206
- methyltransferases
-
spout
-
9-like
-
crenarchaeon
-
2'-o-methylation
- n-methyltransferase
- pyrobaculum
-
pyrococcus
-
n2-guanine
Reaction Schemes
show+
cytidine56 in tRNA
=
+
2'-O-methylcytidine56 in tRNA
Synonyms
atrm56, transfer rna methyltransferase, trm56, pab1040, ta0931, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aTrm56
Ta0931
transfer RNA methyltransferase
Trm56
tRNA ribose 2'-O-methyltransferase aTrm56
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytidine56 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine56-2'-O)-methyltransferase
The archaeal enzyme specifically catalyses the S-adenosyl-L-methionine dependent 2'-O-ribose methylation of cytidine at position 56 in tRNA transcripts.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: in vitro, the tRNA ribose 2'-O-methyltransferase aTrm56 specifically catalyses the AdoMet-dependent 2'-O-ribose methylation of cytidine position 56 in tRNA transcripts. In vitro transcribed Escherichia coli tRNALeu2, yeast tRNAPhe, and Pyrococcus abyssi tRNALeu(CAa) tRNAs are methylated with significant initial rates. Mutations of cytosine at position 56 either by uridine or guanine in tRNA abolish methyl incorporation. A tRNA minisubstrate corresponding to the yeast tRNAAsp transcript missing the D stem-loop, is methylated in vitro at a slightly lower efficiency than the wild-type tRNAAsp. A minisubstrate consisting of the T-loop of tRNAAsp closed by a synthetic stem is also tested. This TSL minisubstrate is still methylated in vitro even though the reaction is 4-5fold less efficient than with the wild type substrate. The complete 3D architecture of the tRNA substrate is not required for aTrm56 catalysis. A T stem-loop structure alone is thus a minimal substrate recognized by aTrm56
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: Pyrococcus horikoshii tRNAVal. aTrm56 prefers the L-shaped tRNA to the lambda form as its substrate
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in elongator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in elongator tRNAMet
Substrates: mature elongator tRNAMet is a better substrate that the precursor of elongator tRNA, which has an intron at the canonical position
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in initiator tRNAMet
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in initiator tRNAMet
Substrates: initiator tRNAMet from Thermoplasma acidophilum strain HO-62 contains G+, m1I, and m22G
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine56 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNALeu(UAG)
Substrates: the methylated nucleotide is identified as pCm
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
additional information
?
-
Substrates: purified Trm56 can methylate the precursor of elongator tRNAMet, which has an intron at the canonical position. But the speed of methyl-transfer by Trm56 to the precursor RNA is considerably slower than that to the mature transcript, which suggests that Trm56 acts mainly on the transcript after the intron has been removed
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Squamous Cell
Transfer RNA methyltransferase gene NSUN2 mRNA expression modifies the effect of T cell activation score on patient survival in head and neck squamous carcinoma.
Neoplasms
Alteration of glycine N-methyltransferase activity in fetal, adult, and tumor tissues.
Neoplasms
Phosphorylation of human TRM9L integrates multiple stress-signaling pathways for tumor growth suppression.
Ovarian Neoplasms
Erratum: Ovarian cancer proliferation and apoptosis are regulated by human transfer RNA methyltransferase 9-like via LIN9.
Ovarian Neoplasms
Ovarian cancer proliferation and apoptosis are regulated by human transfer RNA methyltransferase 9-likevia LIN9.
Vitamin A Deficiency
The effect of vitamin A deficiency on testicular transfer RNA methyltransferase activity.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
additional information
-
Thermoplasma acidophilum grows optimally at 59°C and pH 1.9
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
the enzyme Trm56 is responsible for the typical archaeal tRNA modification of 2'-O-methylcytidine at position 56 (Cm56). The Cm modification is only found at position 56 in native tRNALeuUAG. Trm56 methylates both the elongator tRNAMet transcript and its precursor. But the methyl group acceptance activity of the precursor is considerably lower than that of the mature transcript, the methylation by Trm56 occurs mainly after the removal of the intron
physiological function
-
the enzyme Trm56 is responsible for the typical archaeal tRNA modification of 2'-O-methylcytidine at position 56 (Cm56). The Cm modification is only found at position 56 in native tRNALeuUAG. Trm56 methylates both the elongator tRNAMet transcript and its precursor. But the methyl group acceptance activity of the precursor is considerably lower than that of the mature transcript, the methylation by Trm56 occurs mainly after the removal of the intron
-
physiological function
-
the enzyme Trm56 is responsible for the typical archaeal tRNA modification of 2'-O-methylcytidine at position 56 (Cm56). The Cm modification is only found at position 56 in native tRNALeuUAG. Trm56 methylates both the elongator tRNAMet transcript and its precursor. But the methyl group acceptance activity of the precursor is considerably lower than that of the mature transcript, the methylation by Trm56 occurs mainly after the removal of the intron
-
physiological function
-
the enzyme Trm56 is responsible for the typical archaeal tRNA modification of 2'-O-methylcytidine at position 56 (Cm56). The Cm modification is only found at position 56 in native tRNALeuUAG. Trm56 methylates both the elongator tRNAMet transcript and its precursor. But the methyl group acceptance activity of the precursor is considerably lower than that of the mature transcript, the methylation by Trm56 occurs mainly after the removal of the intron
-
physiological function
-
the enzyme Trm56 is responsible for the typical archaeal tRNA modification of 2'-O-methylcytidine at position 56 (Cm56). The Cm modification is only found at position 56 in native tRNALeuUAG. Trm56 methylates both the elongator tRNAMet transcript and its precursor. But the methyl group acceptance activity of the precursor is considerably lower than that of the mature transcript, the methylation by Trm56 occurs mainly after the removal of the intron
-
additional information
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
additional information
-
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
additional information
-
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
-
additional information
-
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
-
additional information
-
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
-
additional information
-
Trm56 and an yet unknown tRNA (m7G49) methyltransferase might be included in protein complexes and precipitated by centrifugation at 30000 × g. Thermoplasma acidophilum Trm56 might be part of a large complex with other proteins in living cells
-
Show AA Sequence and Transmembrane Helices (901 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of Pyrococcus horikoshii aTrm56 complexed with S-adenosyl-L-methionine at 2.48 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) Rosetta 2 by anion exchange chromatography, heparin affinity chromatography, and gel filtration, followed by dialysis and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Ta0931, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta 2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuratani, M.; Bessho, Y.; Nishimoto, M.; Grosjean, H.; Yokoyama, S.
Crystal structure and mutational study of a unique SpoU family archaeal methylase that forms 2'-O-methylcytidine at position 56 of tRNA
J. Mol. Biol.
375
1064-1075
2008
Pyrococcus horikoshii (O58214), Pyrococcus horikoshii
brenda
Renalier, M.H.; Joseph, N.; Gaspin, C.; Thebault, P.; Mougin, A.
The Cm56 tRNA modification in archaea is catalyzed either by a specific 2'-O-methylase, or a C/D sRNP
RNA
11
1051-1063
2005
Pyrococcus abyssi (Q9UYD1), Pyrococcus abyssi
brenda
Kawamura, T.; Anraku, R.; Hasegawa, T.; Tomikawa, C.; Hori, H.
Transfer RNA methyltransferases from Thermoplasma acidophilum, a thermoacidophilic archaeon
Int. J. Mol. Sci.
16
91-113
2015
Thermoplasma acidophilum (Q9HJN6), Thermoplasma acidophilum, Thermoplasma acidophilum AMRC-C165 (Q9HJN6), Thermoplasma acidophilum ATCC 25905 (Q9HJN6), Thermoplasma acidophilum JCM 9062 (Q9HJN6), Thermoplasma acidophilum NBRC 15155 (Q9HJN6)
brenda
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