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IPR008909 is a DALR anticodon binding.
<p>Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. aaRSs are classified into class I and II (aaRS-I and aaRS-II) based on the topologies of CCDs. Whereas the structure of the CCDs is similar among the members of each of the two different aaRS classes, the ABDs are diverse in structure [[cite:PUB00069766]].</p> <p>The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. Both classes of tRNA synthetases have been subdivided into three subclasses, designated Ia, Ib, Ic and IIa, IIb, IIc.</p> <p>This all α helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. This domain is known as the DALR domain after characteristic conserved amino acids [[cite:PUB00007363]].</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 | Arginine-tRNA ligase activity | Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). | ||
| Molecular function | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Biological process | Arginyl-tRNA aminoacylation | The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: arginine--tRNA ligase, cytoplasmic-like [Cicer arietinum] gi|502164060|ref|XP_004513035.1| | 24 | ||
| – | PREDICTED: arginine--tRNA ligase, cytoplasmic-like isoform X1 [Cicer arietinum] gi|502164143|ref|XP_004513061.1| | 24 | ||
| – | PREDICTED: glycyl-tRNA synthetase 2, chloroplastic/mitochondrial-like [Glycine max] gi|356503250|ref|XP_003520424.1| | 6 | ||
| – | Arginine--tRNA ligase; TAIR: AT4G26300.1 Arginyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O23247|SYRM_ARATH Arginine--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|W0G2X0|W0G2X0_9FABA Arginyl-tRNA synthetase; Found in the gene: LotjaGi2g1v0226300 | 26 | ||
| – | Arginine--tRNA ligase; TAIR: AT4G26300.1 Arginyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O23247|SYRM_ARATH Arginine--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A151T2Z4|A0A151T2Z4_CAJCA Arginyl-tRNA synthetase; Found in the gene: LotjaGi2g1v0226300 | 9 | ||
| – | Arginine--tRNA ligase; TAIR: AT4G26300.5 Arginyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O23247|SYRM_ARATH Arginine--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A072UDN7|A0A072UDN7_MEDTR Cytoplasmic-like arginine-tRNA ligase; Found in the gene: LotjaGi2g1v0226700 | 26 | ||
| – | Arginine--tRNA ligase; TAIR: AT4G26300.1 Arginyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O23247|SYRM_ARATH Arginine--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A151T2Z4|A0A151T2Z4_CAJCA Arginyl-tRNA synthetase; Found in the gene: LotjaGi2g1v0226700 | 9 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF47323 | SUPERFAMILY | 1 | 14.29 |