SMART: DALR_1 domain annotation

DALR_1 DALR anticodon binding domain

SMART accession number:	SM00836
Description:	This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids (PUBMED:10447505).
Family alignment:	View or

There are 1278 DALR_1 domains in 1278 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with DALR_1 domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: translation
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Wolf YI, Aravind L, Grishin NV, Koonin EV
- Evolution of aminoacyl-tRNA synthetases--analysis of unique domainarchitectures and phylogenetic trees reveals a complex history ofhorizontal gene transfer events.
- Genome Res. 1999; 9: 689-710
- Display abstract
- Phylogenetic analysis of aminoacyl-tRNA synthetases (aaRSs) of all 20specificities from completely sequenced bacterial, archaeal, andeukaryotic genomes reveals a complex evolutionary picture. Detailedexamination of the domain architecture of aaRSs using sequence profilesearches delineated a network of partially conserved domains that is evenmore elaborate than previously suspected. Several unexpected evolutionaryconnections were identified, including the apparent origin of thebeta-subunit of bacterial GlyRS from the HD superfamily of hydrolases, adomain shared by bacterial AspRS and the B subunit of archaealglutamyl-tRNA amidotransferases, and another previously undetected domainthat is conserved in a subset of ThrRS, guanosine polyphosphate hydrolasesand synthetases, and a family of GTPases. Comparison of domainarchitectures and multiple alignments resulted in the delineation ofsynapomorphies-shared derived characters, such as extra domains orinserts-for most of the aaRSs specificities. These synapomorphiespartition sets of aaRSs with the same specificity into two or moredistinct and apparently monophyletic groups. In conjunction with clusteranalysis and a modification of the midpoint-rooting procedure, thispartitioning was used to infer the likely root position in phylogenetictrees. The topologies of the resulting rooted trees for most of the aaRSsspecificities are compatible with the evolutionary "standard model"whereby the earliest radiation event separated bacteria from the commonancestor of archaea and eukaryotes as opposed to the two other possibleevolutionary scenarios for the three major divisions of life. For almostall aaRSs specificities, however, this simple scheme is confounded bydisplacement of some of the bacterial aaRSs by their eukaryotic or, lessfrequently, archaeal counterparts. Displacement of ancestral eukaryoticaaRS genes by bacterial ones, presumably of mitochondrial origin, wasobserved for three aaRSs. In contrast, there was no convincing evidence ofdisplacement of archaeal aaRSs by bacterial ones. Displacement of aaRSgenes by eukaryotic counterparts is most common among parasitic andsymbiotic bacteria, particularly the spirochaetes, in which 10 of the 19aaRSs seem to have been displaced by the respective eukaryotic genes andtwo by the archaeal counterpart. Unlike the primary radiation eventsbetween the three main divisions of life, that were readily traceablethrough the phylogenetic analysis of aaRSs, no consistent large-scalebacterial phylogeny could be established. In part, this may be due toadditional gene displacement events among bacterial lineages. Argument ispresented that, although lineage-specific gene loss might have contributedto the evolution of some of the aaRSs, this is not a viable alternative tohorizontal gene transfer as the principal evolutionary phenomenon in thisgene class.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM DALR_1

PDB code	Main view	Title
1bs2		Yeast arginyl-trna synthetase
1f7u		Crystal structure of the arginyl-trna synthetase complexed with the trna(arg) and l-arg
1f7v		Crystal structure of yeast arginyl-trna synthetase complexed with the trnaarg
1iq0		Thermus thermophilus arginyl-trna synthetase
2zue
2zuf
3fnr

DALR_1

3D Structures of DALR_1 domains in PDB