dars-1 Aspartate--tRNA ligase, cytoplasmic [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: dars-1
Official Full Name: Aspartate--tRNA ligase, cytoplasmic
Primary source: WormBase:WBGene00001094
Locus tag: CELE_B0464.1
See related: AllianceGenome:WB:WBGene00001094
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable RNA binding activity and aspartate-tRNA ligase activity. Predicted to be involved in aspartyl-tRNA aminoacylation. Predicted to be located in cytoplasm. Predicted to be part of aminoacyl-tRNA synthetase multienzyme complex. Predicted to be active in cytosol. Orthologous to human DARS1 (aspartyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See dars-1 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 5

Sequence:: Chromosome: III; NC_003281.10 (9489176..9491215, complement)

Chromosome III - NC_003281.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

B0464.1 (e-PCR)
- UniSTS:307187

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables aspartate-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables aspartate-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in aspartyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in aspartyl-tRNA aminoacylation	IEA Inferred from Electronic Annotation more info
involved_in tRNA aminoacylation for protein translation	IEA Inferred from Electronic Annotation more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of aminoacyl-tRNA synthetase multienzyme complex	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Aspartate--tRNA ligase, cytoplasmic

NP_499089.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003281.10 Reference assembly

Range

9489176..9491215 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_066688.4 → NP_499089.1 Aspartate--tRNA ligase, cytoplasmic [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_499089.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q03577

Conserved Domains (3) summary

PLN02850
Location:4 → 531

PLN02850; aspartate-tRNA ligase

cd00776
Location:204 → 527

AsxRS_core; Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as ...

cd04320
Location:84 → 182

AspRS_cyto_N; AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. ...