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Information on EC 2.1.1.268 - tRNAThr (cytosine32-N3)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.268
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.268 tRNAThr (cytosine32-N3)-methyltransferase
IUBMB Comments
The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
The enzyme appears in viruses and cellular organisms
- 2.1.1.268
- actin
-
3-methylcytidine
-
latrunculin
-
filament-binding
- s-adenosylmethionine
-
fission
-
decoding
- cables
Reaction Schemes
show+
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cytosine32 in tRNAThr
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N3-methylcytosine32 in tRNAThr
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cytosine32 in tRNASer
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N3-methylcytosine32 in tRNASer
Synonyms
abp140, trm140, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
m3C32 methyltransferase
METTL2B
Trm140
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
(2)
S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
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S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
(1)
S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNAThr (cytosine32-N3)-methyltransferase
The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
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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 + cytidine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNASer
S-adenosyl-L-methionine + cytidine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNAThr
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr(CGU)
S-adenosyl-L-methionine + cytidine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNASer
Substrates: -
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S-adenosyl-L-methionine + cytidine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNASer
Substrates: isoform METTL2B shows little activity in vitro
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?
S-adenosyl-L-methionine + cytidine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytidine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNAThr
Substrates: isoform METTL2B shows little activity in vitro
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
Substrates: tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
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S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
Substrates: tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation
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S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
Substrates: tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
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S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
Substrates: tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation
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S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
Substrates: tRNAThr1 = tRNAThr(IGU). Trm140p does not have detectable activity on a tRNAThr(IGU) transcript with a C32A mutation. No activity with tRNAPhe. It is demonstrated directly that ABP140 is required for the m3C modification of tRNAThr(IGU) in yeast, and it is infered that ABP140 is required for m3C32 formation for all six tRNAThr and tRNASer species for which m3C is documented
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
-
Substrates: -
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?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: best tRNASer substrate is tRNASer(UGA), lower activity with tRNASer(GCU) and tRNASer(CGA)
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: the enzyme modifies tRNASer species with anticodon sequences UGA, CGA, and GCU
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: best tRNASer substrate is tRNASer(UGA), lower activity with tRNASer(GCU) and tRNASer(CGA)
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
-
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: the enzyme modifies tRNAThr species with anticodon sequences CGU, UGU, and IGU
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?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
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?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr(CGU)
Substrates: G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, overview. Best tRNAThr substrate is tRNATyr(GUA), lower activity occurs with tRNAThr(CGU), tRNAThr(IGU), and tRNAThr(UGU)
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr(CGU)
Substrates: G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, overview. Best tRNAThr substrate is tRNATyr(GUA), lower activity occurs with tRNAThr(CGU), tRNAThr(IGU), and tRNAThr(UGU)
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additional information
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Substrates: compared with isoform METTL2A, METTL2B exhibits dramatically lower activity in vitro. Both G35 and N6-threonylcarbamoyladenosine at position 37 are necessary but insufficient prerequisites for N3-methylcytidine32 in tRNAThr formation, while the anticodon loop and the long variable arm, but not N6-threonylcarbamoyladenosine37, are key determinants for N3-methylcytidine32 in tRNASer(GCU) biogenesis
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additional information
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Substrates: compared with isoform METTL2A, METTL2B exhibits dramatically lower activity in vitro. Both G35 and N6-threonylcarbamoyladenosine at position 37 are necessary but insufficient prerequisites for N3-methylcytidine32 in tRNAThr formation, while the anticodon loop and the long variable arm, but not N6-threonylcarbamoyladenosine37, are key determinants for N3-methylcytidine32 in tRNASer(GCU) biogenesis
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additional information
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Substrates: compared with isoform METTL2A, METTL2B exhibits dramatically lower activity in vitro. Both G35 and N6-threonylcarbamoyladenosine at position 37 are necessary but insufficient prerequisites for N3-methylcytidine32 in tRNAThr formation, while the anticodon loop and the long variable arm, but not N6-threonylcarbamoyladenosine37, are key determinants for N3-methylcytidine32 in tRNASer(GCU) biogenesis
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additional information
?
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Substrates: purified isoform METTL2A is inactive in vitro, or is active but tRNA transcripts are not suitable substrates or needs a cofactor for catalysis
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additional information
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Substrates: purified isoform METTL2A is inactive in vitro, or is active but tRNA transcripts are not suitable substrates or needs a cofactor for catalysis
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additional information
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Substrates: purified isoform METTL2A is inactive in vitro, or is active but tRNA transcripts are not suitable substrates or needs a cofactor for catalysis
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additional information
?
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Substrates: SerRS is essential for the N3-methylcytidine32 biogenesis of human cytoplasmic tRNASer(GCU) by isoform METTL6
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additional information
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Substrates: SerRS is essential for the N3-methylcytidine32 biogenesis of human cytoplasmic tRNASer(GCU) by isoform METTL6
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additional information
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Substrates: SerRS is essential for the N3-methylcytidine32 biogenesis of human cytoplasmic tRNASer(GCU) by isoform METTL6
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additional information
?
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Substrates: isoform METTL8-Iso4 is inactive in N3-methylcytosine32 generation due to the lack of N-extension
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additional information
?
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Substrates: isoform METTL2B exhibits limited methyltransferase activity in vitro (10% compared to isoform METTL2A). G35 is a determinant of isoform METTL2A for N3-methylcytosine32 activity reconstitution. G35 and t6A37 are insufficient for N3-methylcytosine32 modification
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additional information
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Substrates: isoform METTL2B exhibits limited methyltransferase activity in vitro (10% compared to isoform METTL2A). G35 is a determinant of isoform METTL2A for N3-methylcytosine32 activity reconstitution. G35 and t6A37 are insufficient for N3-methylcytosine32 modification
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additional information
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Substrates: isoform METTL2B exhibits limited methyltransferase activity in vitro (10% compared to isoform METTL2A). G35 is a determinant of isoform METTL2A for N3-methylcytosine32 activity reconstitution. G35 and t6A37 are insufficient for N3-methylcytosine32 modification
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additional information
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Substrates: Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
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additional information
?
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Substrates: substrate specificity of enzyme Trm140 in vitro and in vivo, overview. An XGU anticodon and t6A37 are necessary and sufficient for m3C modification of tRNAThr species. tRNAThr(CGU) scaffold used for analysis of tRNAThr variants is fully functional and efficiently modified to m3C. For the tRNAThr(CGU) 28,50 variants, substitution of G35 or U36 with each of the other three nucleotides almost completely abolishes the copurification of tRNA, whereas substitution of C34 with other nucleotides leads to high levels of variant copurification. Trm140 binds tRNAs with a G35-U36 anticodon. G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, activities with tRNAThr variants, overview
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additional information
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Substrates: prior N6-isopentenyladenosine modification of tRNAThr at position A37 is important for N3-methylcytosine32 modification by the enzyme. Prior N6-isopentenyladenosine or threonylcarbamoyladenosine modification of tRNASer at position A37 is important for N3-methylcytosine32 modification by the enzyme
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additional information
?
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Substrates: Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
Products: -
Products: -
?
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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 + cytidine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNASer
Substrates: -
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S-adenosyl-L-methionine + cytidine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytidine32 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
Substrates: tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
Substrates: tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
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Substrates: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: -
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: the enzyme modifies tRNASer species with anticodon sequences UGA, CGA, and GCU
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Substrates: -
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
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Substrates: -
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
Products: -
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: the enzyme modifies tRNAThr species with anticodon sequences CGU, UGU, and IGU
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S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
Substrates: -
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additional information
?
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Substrates: Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
Products: -
Products: -
?
additional information
?
-
Substrates: Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
t6A37 inhibits N3-methylcytosine modification by the enzyme at position 32
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ses1
seryl-tRNA synthetase Ses1 greatly stimulates m3C modification of tRNASer(CGA) and tRNASer(UGA) in vitro
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
subcellular localization of ABP140 to actin filaments is not involved in tRNA modification
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
evolution
malfunction
physiological function
additional information
evolution
in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
evolution
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in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
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malfunction
N3-methylcytosine32 modification is absent in strains that lack the entire ABP140 gene
malfunction
specific reduction of N3-methylcytosine formation in HeLa cells by siRNA-mediated knock down of METTL2B
malfunction
knockout strains in the yeast Saccharomyces cerevisiae lack N3-methylcytosine32 in tRNA1Thr. Lack of the m3C modification does impair translation, albeit mildly
physiological function
N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
physiological function
the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
physiological function
-
isoform METTL8-Iso1 substantially stimulates the aminoacylation activities of SARS2 and TARS2 in vitro, suggesting a functional connection between mitochondrial tRNA modification and charging
physiological function
-
the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
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additional information
enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
additional information
-
enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AB140_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
628
0
71486
Swiss-Prot
-
METL6_HUMAN
284
0
33251
Swiss-Prot
Mitochondrion (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
71486
2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE
71500
2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE
dimer
2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE
monomer
1 * 45400, His6-tagged enzyme, calculated from amino acid sequence
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L155P
the mutant shows about 50% activity compared to the wild type enzyme
P124C
the mutant shows about 10% activity compared to the wild type enzyme
R26S
the mutant shows about 50% activity compared to the wild type enzyme
additional information
additional information
construction of a deletion trm140DELTA strain
additional information
-
construction of a deletion trm140DELTA strain
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells and in HEK-293T cells
expressed in HEK-293T cells and Escherichia coli BL21 (DE3) cells
expression of hexahistidine-tagged Abp140p in Saccharomces cerevisiae
gene ABP140, recombinant expression in Saccharomyces cerevisiae, coexpression with yeast enzyme Ses1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Silva, S.; Haider, S.J.; Phizicky, E.M.
A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop
RNA
17
1100-1110
2011
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae
brenda
Noma, A.; Yi, S.; Katoh, T.; Takai, Y.; Suzuki, T.; Suzuki, T.
Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae
RNA
17
1111-1119
2011
Homo sapiens (Q6P1Q9), Homo sapiens, Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae
brenda
Han, L.; Marcus, E.; DSilva, S.; Phizicky, E.
S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates
RNA
23
406-419
2017
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae ATCC 204508 (Q08641)
brenda
Han, L.; Marcus, E.; Phizicky, E.M.
A semi-quantitative pull-down assay to study tRNA substrate specificity of modification enzymes
Methods Enzymol.
658
359-377
2021
Saccharomyces cerevisiae (Q08641)
brenda
Mao, X.L.; Li, Z.H.; Huang, M.H.; Wang, J.T.; Zhou, J.B.; Li, Q.R.; Xu, H.; Wang, X.J.; Zhou, X.L.
Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6
Nucleic Acids Res.
49
8309-8323
2021
Homo sapiens (Q6P1Q9), Homo sapiens (Q96IZ6), Homo sapiens (Q8TCB7)
brenda
Huang, M.H.; Wang, J.T.; Zhang, J.H.; Mao, X.L.; Peng, G.X.; Lin, X.; Lv, D.; Yuan, C.; Lin, H.; Wang, E.D.; Zhou, X.L.
Mitochondrial RNA m3C methyltransferase METTL8 relies on an isoform-specific N-terminal extension and modifies multiple heterogenous tRNAs
Sci. Bull. (Beijing)
68
2094-2105
2023
Homo sapiens
brenda
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