nars-1 Asparagine--tRNA ligase, cytoplasmic [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: nars-1
Official Full Name: Asparagine--tRNA ligase, cytoplasmic
Primary source: WormBase:WBGene00003815
Locus tag: CELE_F22D6.3
See related: AllianceGenome:WB:WBGene00003815
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 asparagine-tRNA ligase activity. Involved in translation. Predicted to be active in cytoplasm. Orthologous to human NARS1 (asparaginyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See nars-1 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 6

Sequence:: Chromosome: I; NC_003279.8 (7088030..7090062, complement)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

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

F22D6.3 (e-PCR)
- UniSTS:309892

F22D6.4 (e-PCR)
- UniSTS:320509

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables asparagine-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables asparagine-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 asparaginyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in asparaginyl-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
involved_in translation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Asparagine--tRNA ligase, cytoplasmic

NP_001021405.1

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_003279.8 Reference assembly

Range

7088030..7090062 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001026234.8 → NP_001021405.1 Asparagine--tRNA ligase, cytoplasmic [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001021405.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q19722

Conserved Domains (3) summary

COG0017
Location:108 → 545

AsnS; Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]

cd00776
Location:220 → 541

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 ...

cd04323
Location:123 → 206

AsnRS_cyto_like_N; AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a ...