Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR014758 is a Methionyl-tRNA synthetase.
<p>The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [[cite:PUB00079872], [cite:PUB00079873]]. These proteins differ widely in size and oligomeric state, and have limited sequence homology [[cite:PUB00007191]]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [[cite:PUB00006477]]. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [[cite:PUB00000386]], and are mostly dimeric or multimeric, containing at least three conserved regions [[cite:PUB00000723], [cite:PUB00005365], [cite:PUB00004391]]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [[cite:PUB00007363]].</p> <p>Methionine-tRNA ligase ([ec:6.1.1.10]) is an alpha 2 dimer. In some species (archaea, eubacteria and eukaryotes) a coding sequence, similar to the C-terminal end of MetRS, is present as an independent gene which is a tRNA binding domain as a dimer. In eubacteria, MetRS can also be split in two sub-classes corresponding to the presence of one or two CXXC domains specific to zinc binding. The crystal structures of a number of methionine-tRNA ligases are known [[cite:PUB00006477], [cite:PUB00006254], [cite:PUB00006518]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Nucleotide binding | Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. | ||
| Molecular function | Methionine-tRNA ligase activity | Catalysis of the reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). | ||
| Molecular function | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Biological process | Methionyl-tRNA aminoacylation | The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: probable methionyl-tRNA synthetase-like [Glycine max] gi|356543424|ref|XP_003540160.1| | 30 | ||
| – | Methionine-tRNA ligase, putative; TAIR: AT4G13780.1 methionine-tRNA ligase, putative / methionyl-tRNA synthetase, putative / MetRS; Swiss-Prot: sp|Q9ZTS1|SYM_ORYSJ Probable methionine--tRNA ligase; TrEMBL-Plants: tr|A0A0B2SPF8|A0A0B2SPF8_GLYSO Putative methionine--tRNA ligase; Found in the gene: LotjaGi3g1v0538600 | 32 | ||
| – | Methionine-tRNA ligase, putative; TAIR: AT4G13780.1 methionine-tRNA ligase, putative / methionyl-tRNA synthetase, putative / MetRS; Swiss-Prot: sp|Q9ZTS1|SYM_ORYSJ Probable methionine--tRNA ligase; TrEMBL-Plants: tr|A0A0R0H9H8|A0A0R0H9H8_SOYBN Uncharacterized protein; Found in the gene: LotjaGi3g1v0538600 | 24 | ||
| – | Methionine-tRNA ligase, putative; TAIR: AT4G13780.1 methionine-tRNA ligase, putative / methionyl-tRNA synthetase, putative / MetRS; Swiss-Prot: sp|Q9ZTS1|SYM_ORYSJ Probable methionine--tRNA ligase; TrEMBL-Plants: tr|A0A0R0H0Q5|A0A0R0H0Q5_SOYBN Uncharacterized protein; Found in the gene: LotjaGi3g1v0538600 | 24 | ||
| – | Methionine--tRNA ligase; TAIR: AT3G55400.1 methionyl-tRNA synthetase / methionine-tRNA ligase / MetRS (cpMetRS); Swiss-Prot: sp|Q9M2T9|SYMM_ARATH Methionine--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A0S3SL75|A0A0S3SL75_PHAAN Uncharacterized protein; Found in the gene: LotjaGi5g1v0029200 | 27 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd07957 | CDD | 1 | 20.00 |