6.1.1.18: glutamine-tRNA ligase
This is an abbreviated version!
For detailed information about glutamine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.18
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6.1.1.18
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synthetases
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aminoacyl-trna
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aminoacylation
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anticodon
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glutamyl-trna
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glutaminylation
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gln-trnagln
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noncognate
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aarss
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trna-dependent
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mischarging
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transamidation
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asnrs
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aspartyl-trna
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trna2gln
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nondiscriminating
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trnatyr
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misaminoacylation
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glurss
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misacylated
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ilers
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cysrs
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anticodon-binding
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valrs
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gatcab
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gln-trna
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drug development
- 6.1.1.18
- synthetases
- aminoacyl-trna
- aminoacylation
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anticodon
- glutamyl-trna
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glutaminylation
- gln-trnagln
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noncognate
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aarss
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trna-dependent
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mischarging
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transamidation
- asnrs
- aspartyl-trna
- trna2gln
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nondiscriminating
- trnatyr
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misaminoacylation
- glurss
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misacylated
- ilers
- cysrs
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anticodon-binding
- valrs
- gatcab
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gln-trna
- drug development
Reaction
Synonyms
class I glutaminyl-tRNA synthetase, cytosolic glutaminyl-tRNA synthetase, Gln-RS, Gln4, GlnRS, Glutamine translase, Glutamine--tRNA ligase, Glutamine-tRNA synthetase, glutaminyl tRNA synthetase, Glutaminyl-transfer ribonucleate synthetase, Glutaminyl-transfer RNA synthetase, Glutaminyl-tRNA synthetase, glutaminyltRNA synthetase, glutamyl/glutaminyl-tRNA synthetase, QARS, QRS, Synthetase, glutaminyl-transfer ribonucleate, Vegetative specific protein H4
ECTree
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Subunits
Subunits on EC 6.1.1.18 - glutamine-tRNA ligase
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monomer
additional information
monomer
the enzyme adopts a boomerang-like shaped structure built of 5 domains, domain organization of the intact enzyme and structure of the functionally important N-terminal domain, modeling of overall structure and domain organization of wild-type, full-length enzyme, structure-function analysis, overview
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
additional information
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the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
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additional information
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
GlnRS structure networks, detection method development for accounting side chain interactions, yet providing a global view of the ligand-induced conformational changes, and understand allosteric changes mediated by the binding of ligands, usage of crystal structures: PDB IDs 1nyl, 1qtq, 1o0b, and 1o0c, overview
additional information
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GlnRS structure networks, detection method development for accounting side chain interactions, yet providing a global view of the ligand-induced conformational changes, and understand allosteric changes mediated by the binding of ligands, usage of crystal structures: PDB IDs 1nyl, 1qtq, 1o0b, and 1o0c, overview
additional information
molecular dynamics simulations on wild-type tRNA, var-AGGUtRNA, and tRNA-GlnRS complexes, overview
additional information
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long-range signal propagation from the tRNA anticodon is dynamically driven, whereas shorter pathways are mediated by induced-fit rearrangements, structure modelling, overview
additional information
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targeting into the multienzyme complex is mediated by the C-terminal catalytic domain
additional information
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
in the multisynthetase complex (MSC) subcomplex (RQA1 subcomplex) comprising arginyl-tRNA synthetase (ArgRS), glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 ((AIMP1)/p43), the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. The MSC complex is comprised of nine different aminoacyl-tRNA synthetases (ARSs) and three accessary proteins. This ternary RQA1 complex is further anchores to AIMP2/p38 through interaction with AIMP1. Importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the assembly of the higher-order MSC protein complex. The N-terminal domain of human GlnRS interacts with ArgRS in the MSC, GlnRS is anchored to the complex by the interaction of its C-terminal core with the Hb helix of ArgRS, structure-function analysis, overview. ArgRS, GlnRS, and AIMP1 form a 1:1:1 ternary complex in the asymmetric unit, besides a trimeric, the RQA1 subcomplex also can form a hexameric structure
additional information
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enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure, that can be visualized by electron microscopy
additional information
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
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determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
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Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
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