2.1.1.220: tRNA (adenine58-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (adenine58-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.220
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2.1.1.220
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trnaimet
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1-methyladenosine
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nucleoside
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mtases
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two-subunit
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thermus
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exosome
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polyadenylation
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adomet
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t-loop
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polya
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s-adenosylmethionine
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n1-methylation
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heterotetramer
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homotetrameric
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methionyl-trna
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high-copy-number
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eubacteria
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methyltransferases
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s-adenosyl-l-homocysteine
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two-component
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s-adenosyl-l-methionine-dependent
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l-shaped
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tpsic
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trna-binding
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hypomodified
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drug development
- 2.1.1.220
- trnaimet
- 1-methyladenosine
- nucleoside
- mtases
-
two-subunit
-
thermus
-
exosome
-
polyadenylation
- adomet
-
t-loop
- polya
- s-adenosylmethionine
-
n1-methylation
- heterotetramer
-
homotetrameric
- methionyl-trna
-
high-copy-number
- eubacteria
- methyltransferases
- s-adenosyl-l-homocysteine
-
two-component
-
s-adenosyl-l-methionine-dependent
-
l-shaped
-
tpsic
-
trna-binding
-
hypomodified
- drug development
Reaction
Synonyms
EC 2.1.1.36, Gcd10p, Gcd10p-Gcd14p, Gcd10pyGcd14p complex, Gcd14p, m1A58 MTase, m1A58 tRNA methyl-transferase, m1A58 tRNA methyltransferase, m1A58-methyltransferase, m1A58MTase, Rv2118c, Rv2118p, Trm6, TRM6-TRM61 holoenzyme, Trm61A, Trm61B, TRm61p, TRm6p, TrmI, tRNA (m1A58) methyltransferase, tRNA (m1A58) MTase, tRNA m(1)A58 methyltransferase, tRNA m1A58 methyltransferase, two component m1A58 tRNA methyl-transferase
ECTree
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Subunits
Subunits on EC 2.1.1.220 - tRNA (adenine58-N1)-methyltransferase
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x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation
heterodimer
heterotetramer
homotetramer
tetramer
additional information
P41814; P46959
TRM6 and TRM61 form a compact complex via numerous hydrogen bonding and extensive hydrophobic interactions. The heterodimer interface of TRM6-TRM61 buries 3194 A2 of TRM6 and 3167 A2 of TRM61 solvent-accessible area, which represents about 17% and 16% of TRM6 and TRM61's total surface area, respectively. TRM6 mainly interacts with TRM61 through four major sites. Interaction analyses for sites A-C, detailed overview
heterodimer
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TRM6 and TRM61 form a compact complex via numerous hydrogen bonding and extensive hydrophobic interactions. The heterodimer interface of TRM6-TRM61 buries 3194 A2 of TRM6 and 3167 A2 of TRM61 solvent-accessible area, which represents about 17% and 16% of TRM6 and TRM61's total surface area, respectively. TRM6 mainly interacts with TRM61 through four major sites. Interaction analyses for sites A-C, detailed overview
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dimers of tightly assembled heterodimers, formed by TrmI-6 and TrmI-61 subunits, interactions and structure analysis, overview
heterotetramer
the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer
heterotetramer
P41814; P46959
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
heterotetramer
P41814; P46959
two TRM6-TRM61 heterodimers assemble as a heterotetramer. A symmetric unit of the TRM6-TRM61 crystal contains one molecule of TRM6 and one molecule of TRM61, forming a 1:1 heterodimer. TRM6 and TRM61 form a 2:2 tetrameric heterocomplex, displaying an omega shape. Two symmetry-related TRM6-TRM61 heterodimer come together to form a central beta-barrel structure that consists of beta13 (TRM6), loop beta13/beta14 (TRM6), beta12(TRM61) and loop beta13/beta14 (TRM61). The top of the barrel contains a hydrophobic core, formed by residues Tyr422 (TRM6), Pro431 (TRM6), Met253 (TRM61), His354 (TRM61), and Tyr357 (TRM61) The center of the barrel is filled with numerous hydrophilic side-chains, including residues Glu416 (TRM6), Arg418 (TRM6), Arg420 (TRM6), Glu255 (TRM61), Gln257 (TRM61) and Arg259 (TRM61). The bottom of the barrel consists of a cage of four tyrosine residues. Modelling of the heterotetramer interface of TRM6-TRM61, overview. A TRM6-TRM61 heterotetramer constitutes two L-shaped tRNA binding regions. Structure comparison to the enzyme from Homo sapiens
heterotetramer
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two TRM6-TRM61 heterodimers assemble as a heterotetramer. A symmetric unit of the TRM6-TRM61 crystal contains one molecule of TRM6 and one molecule of TRM61, forming a 1:1 heterodimer. TRM6 and TRM61 form a 2:2 tetrameric heterocomplex, displaying an omega shape. Two symmetry-related TRM6-TRM61 heterodimer come together to form a central beta-barrel structure that consists of beta13 (TRM6), loop beta13/beta14 (TRM6), beta12(TRM61) and loop beta13/beta14 (TRM61). The top of the barrel contains a hydrophobic core, formed by residues Tyr422 (TRM6), Pro431 (TRM6), Met253 (TRM61), His354 (TRM61), and Tyr357 (TRM61) The center of the barrel is filled with numerous hydrophilic side-chains, including residues Glu416 (TRM6), Arg418 (TRM6), Arg420 (TRM6), Glu255 (TRM61), Gln257 (TRM61) and Arg259 (TRM61). The bottom of the barrel consists of a cage of four tyrosine residues. Modelling of the heterotetramer interface of TRM6-TRM61, overview. A TRM6-TRM61 heterotetramer constitutes two L-shaped tRNA binding regions. Structure comparison to the enzyme from Homo sapiens
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homotetramer
bacterial and archaeal TrmI proteins have been shown to form homotetramers. Each homotetramers accomodates up to two tRNA molecules
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dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, interactions and structure analysis, overview
tetramer
dimer of heterodimers in which each heterodimer comprises a catalytic chain, Trm61, and a homologous but noncatalytic chain, Trm6, repurposed as a tRNA-binding subunit that acts in trans, crystal structure analysis
tetramer
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dimers of tightly assembled dimers, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, and the tetramer is strengthened by four intersubunit disulfide bridges, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview
tetramer
4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p)
tetramer
the enzyme remains tetrameric upon tRNA binding, with formation of complexes involving one to two molecules of tRNA per TrmI tetramer
tetramer
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dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview
tetramer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p)
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additional information
Trm6 is less conserved with respect to TrmI than Trm61 and lacks a cofactor-binding pocket, enzyme quaternary structure, overview
additional information
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Trm6 is less conserved with respect to TrmI than Trm61 and lacks a cofactor-binding pocket, enzyme quaternary structure, overview
additional information
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
additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
additional information
P46959; P41814
Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate
additional information
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Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate
additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview