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Literature summary extracted from

  • Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
    m1A Post-transcriptional modification in tRNAs (2017), Biomolecules, 7, 20 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.218 crystal structure PDB ID 5A7T Thermococcus kodakarensis
2.1.1.218 crystal structure PDB ID 5A7T Sulfolobus acidocaldarius
2.1.1.220 crystal structure is available for heterotetrameric Trm6-Trm61A complex from Saccharomyces cerevisiae Saccharomyces cerevisiae
2.1.1.220 crystal structure of the human m1A58 MTase in complex with tRNALys3 (PDB ID 5CCB), and of human complex Trm6-Trm61 (PDB ID 2B25) Homo sapiens
2.1.1.221 crystal structure PDB ID 4FMW Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.220 cytosol two subunits Trm6-Trm61 Saccharomyces cerevisiae 5829
-
2.1.1.220 cytosol two subunits Trm6-Trm61 Homo sapiens 5829
-
2.1.1.220 mitochondrion only subunit Trm61 Saccharomyces cerevisiae 5739
-
2.1.1.220 mitochondrion only subunit Trm61 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA Streptococcus pneumoniae
-
 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA Vibrio cholerae
-
 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA Listeria monocytogenes serotype 4b
-
 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA Staphylococcus aureus
-
 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA Listeria monocytogenes serotype 4b LL195
-
 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Thermococcus kodakarensis
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Thermococcus kodakarensis JCM 12380
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius DSM 639
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Thermococcus kodakarensis ATCC BAA-918
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius ATCC 33909
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius NBRC 15157
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius NCIMB 11770
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius JCM 8929
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA Thermus thermophilus
-
 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA Saccharomyces cerevisiae
-
 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA Homo sapiens
-
 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNALys3 Saccharomyces cerevisiae
-
 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNALys3 Homo sapiens
-
 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Thermococcus kodakarensis
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Schizosaccharomyces pombe
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Thermococcus kodakarensis JCM 12380
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Schizosaccharomyces pombe ATCC 24843
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Schizosaccharomyces pombe 972
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Saccharomyces cerevisiae ATCC 204508
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA Thermococcus kodakarensis ATCC BAA-918
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.217 Listeria monocytogenes serotype 4b A0A0E1R6X8
-
-
2.1.1.217 Listeria monocytogenes serotype 4b LL195 A0A0E1R6X8
-
-
2.1.1.217 Staphylococcus aureus A0A0D6HIR7
-
-
2.1.1.217 Streptococcus pneumoniae
-
-
-
2.1.1.217 Vibrio cholerae A0A0H6U323
-
-
2.1.1.218 Homo sapiens Q7L0Y3
-
-
2.1.1.218 Sulfolobus acidocaldarius Q4J894
-
-
2.1.1.218 Sulfolobus acidocaldarius ATCC 33909 Q4J894
-
-
2.1.1.218 Sulfolobus acidocaldarius DSM 639 Q4J894
-
-
2.1.1.218 Sulfolobus acidocaldarius JCM 8929 Q4J894
-
-
2.1.1.218 Sulfolobus acidocaldarius NBRC 15157 Q4J894
-
-
2.1.1.218 Sulfolobus acidocaldarius NCIMB 11770 Q4J894
-
-
2.1.1.218 Thermococcus kodakarensis Q5JD38
-
-
2.1.1.218 Thermococcus kodakarensis ATCC BAA-918 Q5JD38
-
-
2.1.1.218 Thermococcus kodakarensis JCM 12380 Q5JD38
-
-
2.1.1.220 Homo sapiens Q9UJA5 AND Q96FX7 AND Q9BVS5 subunits Trm6, Trm61A and Trm61B
-
2.1.1.220 Saccharomyces cerevisiae P41814 AND P46959 subunits Trm6 and Trm61,or GCD10 and GCD14, respectively
-
2.1.1.220 Thermus thermophilus Q8GBB2
-
-
2.1.1.221 Homo sapiens Q7L0Y3
-
-
2.1.1.221 Homo sapiens Q8TBZ6
-
-
2.1.1.221 Saccharomyces cerevisiae Q12400
-
-
2.1.1.221 Saccharomyces cerevisiae ATCC 204508 Q12400
-
-
2.1.1.221 Schizosaccharomyces pombe O14214
-
-
2.1.1.221 Schizosaccharomyces pombe 972 O14214
-
-
2.1.1.221 Schizosaccharomyces pombe ATCC 24843 O14214
-
-
2.1.1.221 Thermococcus kodakarensis Q5JD38
-
-
2.1.1.221 Thermococcus kodakarensis ATCC BAA-918 Q5JD38
-
-
2.1.1.221 Thermococcus kodakarensis JCM 12380 Q5JD38
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA
-
 Streptococcus pneumoniae S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA
-
 Vibrio cholerae S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA
-
 Listeria monocytogenes serotype 4b S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA
-
 Staphylococcus aureus S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.217 S-adenosyl-L-methionine + adenine22 in tRNA
-
 Listeria monocytogenes serotype 4b LL195 S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
-
 ?
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius ?
-
-
2.1.1.218 additional information the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Homo sapiens ?
-
-
2.1.1.218 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis ?
-
-
2.1.1.218 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis JCM 12380 ?
-
-
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius DSM 639 ?
-
-
2.1.1.218 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis ATCC BAA-918 ?
-
-
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius ATCC 33909 ?
-
-
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius NBRC 15157 ?
-
-
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius NCIMB 11770 ?
-
-
2.1.1.218 additional information the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 Sulfolobus acidocaldarius JCM 8929 ?
-
-
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Thermococcus kodakarensis S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Thermococcus kodakarensis JCM 12380 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius DSM 639 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Thermococcus kodakarensis ATCC BAA-918 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius ATCC 33909 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius NBRC 15157 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius NCIMB 11770 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.218 S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius JCM 8929 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Thermus thermophilus 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Saccharomyces cerevisiae 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Homo sapiens 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNALys3
-
 Saccharomyces cerevisiae 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
-
 ?
2.1.1.220 2 S-adenosyl-L-methionine + adenine58 in tRNALys3
-
 Homo sapiens 2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
-
 ?
2.1.1.221 additional information the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Homo sapiens ?
-
-
2.1.1.221 additional information the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Homo sapiens ?
-
-
2.1.1.221 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis ?
-
-
2.1.1.221 additional information the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Saccharomyces cerevisiae ?
-
-
2.1.1.221 additional information the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Schizosaccharomyces pombe ?
-
-
2.1.1.221 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis JCM 12380 ?
-
-
2.1.1.221 additional information the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Schizosaccharomyces pombe ATCC 24843 ?
-
-
2.1.1.221 additional information the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Schizosaccharomyces pombe 972 ?
-
-
2.1.1.221 additional information the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 Saccharomyces cerevisiae ATCC 204508 ?
-
-
2.1.1.221 additional information the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA Thermococcus kodakarensis ATCC BAA-918 ?
-
-
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Thermococcus kodakarensis S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Schizosaccharomyces pombe S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Thermococcus kodakarensis JCM 12380 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Schizosaccharomyces pombe ATCC 24843 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Schizosaccharomyces pombe 972 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
2.1.1.221 S-adenosyl-L-methionine + guanine9 in tRNA
-
 Thermococcus kodakarensis ATCC BAA-918 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.220 heterotetramer the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer Homo sapiens
2.1.1.220 heterotetramer the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer. In the complex of Trm6-Trm61 from Saccharomyces cerevisiae, both subunits harbour an N-terminal domain linked to a C-terminal domain. The C-terminal domains cover a Rossmann-fold and are very similar between the two subunits, whereas significant differences are found between the N-terminal domains. The N-terminal domain of Trm61 contains a short alpha-helix and three hairpin beta-motifs, whereas Trm6 consists of a short alpha-helix with seven antiparallel beta-strands and a highly flexible region with a number of positively-charged residues. Each subunit of the Trm6-Trm61 complex forms heterodimers that, again, assemble as a heterotetramer. The catalytic subunit of this complex (Trm61) binds the cofactor SAM, a binding that is made impossible in the other subunit (Trm6) by the loss of conserved motifs involved in accommodation of this cofactor. Each heterotetramer binds two tRNA molecules onto two distal, L-shaped surfaces on the protein complex Saccharomyces cerevisiae
2.1.1.220 homotetramer bacterial and archaeal TrmI proteins have been shown to form homotetramers. Each homotetramers accomodates up to two tRNA molecules Thermus thermophilus
2.1.1.220 More in mitochondria, MTase Trmt61B forms a tetramer, presumed to resemble the homotetramers of TrmI proteins. In support of a similar structural arrangement between Trmt61B and TrmI, a phylogenetic analysis confirmed a bacterial origin of the human protein Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.1.1.217 m1A22 MTase
-
 Streptococcus pneumoniae
2.1.1.217 m1A22 MTase
-
 Vibrio cholerae
2.1.1.217 m1A22 MTase
-
 Listeria monocytogenes serotype 4b
2.1.1.217 m1A22 MTase
-
 Staphylococcus aureus
2.1.1.217 TrmK
-
 Streptococcus pneumoniae
2.1.1.217 TrmK
-
 Vibrio cholerae
2.1.1.217 TrmK
-
 Listeria monocytogenes serotype 4b
2.1.1.217 TrmK
-
 Staphylococcus aureus
2.1.1.218 m1A9 MTase
-
 Sulfolobus acidocaldarius
2.1.1.218 More see also EC 2.1.1.221 Thermococcus kodakarensis
2.1.1.218 More see also EC 2.1.1.221 Homo sapiens
2.1.1.218 SPOUT MTase
-
 Thermococcus kodakarensis
2.1.1.218 SPOUT MTase
-
 Sulfolobus acidocaldarius
2.1.1.218 SPOUT MTase
-
 Homo sapiens
2.1.1.218 Trm10
-
 Thermococcus kodakarensis
2.1.1.218 Trm10
-
 Sulfolobus acidocaldarius
2.1.1.218 Trmt10C
-
 Homo sapiens
2.1.1.220 m1A58 MTase
-
 Thermus thermophilus
2.1.1.220 m1A58 MTase
-
 Saccharomyces cerevisiae
2.1.1.220 m1A58 MTase
-
 Homo sapiens
2.1.1.220 Trm6
-
 Saccharomyces cerevisiae
2.1.1.220 Trm6
-
 Homo sapiens
2.1.1.220 Trm61A
-
 Saccharomyces cerevisiae
2.1.1.220 Trm61A
-
 Homo sapiens
2.1.1.220 Trm61B
-
 Saccharomyces cerevisiae
2.1.1.220 Trm61B
-
 Homo sapiens
2.1.1.220 TrmI
-
 Thermus thermophilus
2.1.1.221 m1G9 MTase
-
 Saccharomyces cerevisiae
2.1.1.221 m1G9 MTase
-
 Schizosaccharomyces pombe
2.1.1.221 m1G9 MTase
-
 Homo sapiens
2.1.1.221 More see also EC 2.1.1.218 Thermococcus kodakarensis
2.1.1.221 More see also EC 2.1.1.218 Homo sapiens
2.1.1.221 SPOUT MTase
-
 Thermococcus kodakarensis
2.1.1.221 SPOUT MTase
-
 Saccharomyces cerevisiae
2.1.1.221 SPOUT MTase
-
 Homo sapiens
2.1.1.221 Trm10
-
 Thermococcus kodakarensis
2.1.1.221 Trm10
-
 Schizosaccharomyces pombe
2.1.1.221 TRMT10A
-
 Saccharomyces cerevisiae
2.1.1.221 TRMT10A
-
 Homo sapiens
2.1.1.221 Trmt10C
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.217 S-adenosyl-L-methionine
-
 Streptococcus pneumoniae
2.1.1.217 S-adenosyl-L-methionine
-
 Vibrio cholerae
2.1.1.217 S-adenosyl-L-methionine
-
 Listeria monocytogenes serotype 4b
2.1.1.217 S-adenosyl-L-methionine
-
 Staphylococcus aureus
2.1.1.218 S-adenosyl-L-methionine
-
 Thermococcus kodakarensis
2.1.1.218 S-adenosyl-L-methionine
-
 Sulfolobus acidocaldarius
2.1.1.218 S-adenosyl-L-methionine
-
 Homo sapiens
2.1.1.220 S-adenosyl-L-methionine
-
 Thermus thermophilus
2.1.1.220 S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae
2.1.1.220 S-adenosyl-L-methionine
-
 Homo sapiens
2.1.1.221 S-adenosyl-L-methionine
-
 Thermococcus kodakarensis
2.1.1.221 S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae
2.1.1.221 S-adenosyl-L-methionine
-
 Schizosaccharomyces pombe
2.1.1.221 S-adenosyl-L-methionine
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 Homo sapiens

General Information

EC Number General Information Comment Organism
2.1.1.217 evolution the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria Streptococcus pneumoniae
2.1.1.217 evolution the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria Vibrio cholerae
2.1.1.217 evolution the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria Listeria monocytogenes serotype 4b
2.1.1.217 evolution the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria Staphylococcus aureus
2.1.1.217 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding Streptococcus pneumoniae
2.1.1.217 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding Vibrio cholerae
2.1.1.217 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding Listeria monocytogenes serotype 4b
2.1.1.217 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding Staphylococcus aureus
2.1.1.217 physiological function the enzyme is essential for the bacterial survival Streptococcus pneumoniae
2.1.1.217 physiological function the enzyme is essential for the bacterial survival Vibrio cholerae
2.1.1.217 physiological function the enzyme is essential for the bacterial survival Listeria monocytogenes serotype 4b
2.1.1.217 physiological function the enzyme is essential for the bacterial survival Staphylococcus aureus
2.1.1.218 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Thermococcus kodakarensis
2.1.1.218 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Sulfolobus acidocaldarius
2.1.1.218 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Homo sapiens
2.1.1.218 malfunction mutation of catalytic residue Asp184 abolishes m1A9 activity in the archaeal Trm10 protein Sulfolobus acidocaldarius
2.1.1.218 malfunction mutation of catalytic residue Asp206 abolishes m1A9 activity in the archaeal Trm10 protein Thermococcus kodakarensis
2.1.1.218 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Thermococcus kodakarensis
2.1.1.218 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Sulfolobus acidocaldarius
2.1.1.218 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Homo sapiens
2.1.1.218 additional information in human Trmt10C, the catalytic aspartate residue, found in archaeal m1A9 MTases, is replaced by leucine that, due to its uncharged nature, is likely to act differently in catalysis than a charged aspartate residue. Another aspartate residue is located deep in the active site pocket of human Trmt10C (Asp293) and might be involved in catalysis, but seems unlikely to be the determinant for m1A9 activity, as this position is occupied by aspartate in the m1G9-specific Trm10 proteins from yeast, and is not conserved in m1A9 active Trm10 proteins from Sulfolobus acidocaldarius and Thermococcus kodakarensis. tRNA recognition by Trm10 enzymes, overview Homo sapiens
2.1.1.218 additional information tRNA recognition by Trm10 enzymes, overview Thermococcus kodakarensis
2.1.1.218 additional information tRNA recognition by Trm10 enzymes, overview Sulfolobus acidocaldarius
2.1.1.220 evolution the m1A58 modification occurs on (cyt)tRNAs from all three domains of life and further in (mt)tRNAs. The enzyme belongs to the RFM class I methyltransferases. In eukaryotes, the m1A58 MTase located in the cytosol is composed of a catalytic protein unit from the Trm61 subfamily (Trm61A) and an RNA-binding protein unit from the Trm6 subfamily (Trm6). Trm6 and Trm61 share a common ancestor and arose via gene duplication and divergent evolution. The mitochondrial m1A58 MTase consists of a single protein from the Trm61 family (Trmt61B), which is a paralogue to Trm61A from the cytosolic complex Saccharomyces cerevisiae
2.1.1.220 evolution the m1A58 modification occurs on (cyt)tRNAs from all three domains of life and further in (mt)tRNAs. The enzyme belongs to the RFM class I methyltransferases. In eukaryotes, the m1A58 MTase located in the cytosol is composed of a catalytic protein unit from the Trm61 subfamily (Trm61A) and an RNA-binding protein unit from the Trm6 subfamily (Trm6). Trm6 and Trm61 share a common ancestor and arose via gene duplication and divergent evolution. The mitochondrial m1A58 MTase consists of a single protein from the Trm61 family (Trmt61B), which is a paralogue to Trm61A from the cytosolic complex. In mitochondria, MTase Trmt61B forms a tetramer, presumed to resemble the homotetramers of TrmI proteins. In support of a similar structural arrangement between Trmt61B and TrmI, a phylogenetic analysis confirmed a bacterial origin of the human protein Homo sapiens
2.1.1.220 evolution the m1A58 modification occurs on (cyt)tRNAs from all three domains of life and further in (mt)tRNAs. The m1A58 MTases belong to the RFM methyltransferase superfamily, class I. In archaea and bacteria, the m1A58 MTases belong to the TrmI subfamily and function without complex partners Thermus thermophilus
2.1.1.220 malfunction deletion of the MTase N1-methylation A58 in yeast produces non-viable cells Saccharomyces cerevisiae
2.1.1.220 malfunction the lack of m1A58 in human tRNALys3 has been shown to be crucial for reverse transcription fidelity and efficiency of retroviruses like HIV-1. The lack of m1A58 results in an abnormal tRNAi structure, guiding it for degradation. This might explain why exclusion of this MTase by siRNA-mediated knockdown gives rise to a slow-growth phenotype in human cells Homo sapiens
2.1.1.220 malfunction the lack of the enzyme forming m1A58 leads to thermosensitivity in bacterial tRNAs Thermus thermophilus
2.1.1.220 metabolism in cytosolic (cyt) tRNA, the m1A modification occurs at five different positions (9, 14, 22, 57, and 58), two of which (9 and 58) are also found in mitochondrial (mt) tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. Two enzyme families are responsible for formation of m1A at nucleotide position 9 and 58 in tRNA, tRNA binding, m1A mechanism, protein domain organisation and overall structures Homo sapiens
2.1.1.220 metabolism in cytosolic (cyt) tRNA, the m1A modification occurs at five different positions (9, 14, 22, 57, and 58), two of which (9 and 58) are also found in mitochondrial tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. Two enzyme families are responsible for formation of m1A at nucleotide position 9 and 58 in tRNA, tRNA binding, m1A mechanism, protein domain organisation and overall structures Saccharomyces cerevisiae
2.1.1.220 additional information catalytic mechanism of m1A58 specific RFM family member TrmI, overview. The conserved aspartate residue (Asp181) is essential for m1A58 MTase activity in Thermus thermophilus Thermus thermophilus
2.1.1.220 additional information crystal structure of the human m1A58 MTase in complex with tRNALys3 have not provided information on the correct mechanism, as the position of A58 in the active site resembles a methylated nucleobase in a product-complex Homo sapiens
2.1.1.220 additional information crystal structure of the human m1A58 MTase in complex with tRNALys3 have not provided information on the correct mechanism, as the position of A58 in the active site resembles a methylated nucleobase in a product-complex. tRNA undergoes large conformational changes during binding in which the D- and T-arm are separated. The T-loop contains the nucleobase to be modified (A58) and binds in the active site. The binding is stabilised by the formation of numerous hydrogen bonds with the C56 nucleobase and the sugar-phosphate backbone. A stabilising hydrogen bond is also formed between a phosphate O atom of C56 and a H atom of the exocyclic N6 atom of A58. No hydrogen bonds are observed between the protein complex and A58, and the orientation of this adenosine towards the bound S-adenosyl-L-homocysteine (SAH) resembles a methylated nucleobase. A conserved aspartate residue (Asp181) is found in close proximity to A58 and could serve as the catalytic base. The complex makes additional contacts with the tRNA substrate with binding of the acceptor stem to the N?terminal domain of the catalytic subunit Trm61, and binding of the T?stem/loop to an insert in the N?terminal domain of Trm6, not present in Trm61. The vast number of interactions with both complex subunits explain previous findings that both Trm6 and Trm61 are required for tRNA binding. The interactions between tRNA and Trm6 help orient A58 for catalysis and may contribute to target specificity, providing a role for the non?catalytic subunit Trm6 in activity Saccharomyces cerevisiae
2.1.1.220 physiological function the m1A58 modifications have both been linked to structural stability and/or correct folding of the tRNA and is related to structural thermostability of tRNA, role of m1A58 in tRNAi structure stability. m1A58 is important for maturation of the initiator tRNAMet from yeast. The initiator tRNA from eukaryotes (tRNAi) has a conserved A-rich T-loop (A54, A58, and A69), a conserved A20 and a shorter-than-average D-loop (seven nucleobases). These features cluster in the corner of the L-shaped tRNA and the structure is maintained by a dense network of hydrogen bonds between the conserved adenines. In this network, A58 forms hydrogen bonds to A54 and A60 Saccharomyces cerevisiae
2.1.1.220 physiological function the m1A58 modifications have both been linked to structural stability and/or correct folding of the tRNA and is related to structural thermostability of tRNA, role of m1A58 in tRNAi structure stability. The initiator tRNA from eukaryotes (tRNAi) has a conserved A-rich T-loop (A54, A58, and A69), a conserved A20 and a shorter-than-average D-loop (seven nucleobases). These features cluster in the corner of the L-shaped tRNA and the structure is maintained by a dense network f hydrogen bonds between the conserved adenines. In this network, A58 forms hydrogen bonds to A54 and A60 Homo sapiens
2.1.1.220 physiological function the m1A58 modifications have both been linked to structural stability and/or correct folding of the tRNA and is related to structural thermostability of tRNA. The combination of m1A58 with two other post-transcriptional modifications (Gm18 and m5s2U54) increases the melting temperature of tRNAs from Thermus thermophilus by approximately 10°C compared to the unmodified transcript Thermus thermophilus
2.1.1.221 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Thermococcus kodakarensis
2.1.1.221 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Saccharomyces cerevisiae
2.1.1.221 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Schizosaccharomyces pombe
2.1.1.221 evolution aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein Homo sapiens
2.1.1.221 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Thermococcus kodakarensis
2.1.1.221 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Saccharomyces cerevisiae
2.1.1.221 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Schizosaccharomyces pombe
2.1.1.221 metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms Homo sapiens
2.1.1.221 additional information tRNA recognition by Trm10 enzymes, overview Thermococcus kodakarensis
2.1.1.221 additional information tRNA recognition by Trm10 enzymes, overview Saccharomyces cerevisiae
2.1.1.221 additional information tRNA recognition by Trm10 enzymes, overview Schizosaccharomyces pombe
2.1.1.221 additional information tRNA recognition by Trm10 enzymes, overview Homo sapiens