U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

DUS2 dihydrouridine synthase 2 [ Lagenorhynchus obliquidens (Pacific white-sided dolphin) ]

Gene ID: 113627170, updated on 15-Mar-2024

Summary

Go to the top of the page Help
Gene symbol
DUS2
Gene description
dihydrouridine synthase 2
See related
EnsemblRapid:ENSLOBG00000003293
Gene type
protein coding
RefSeq status
MODEL
Organism
Lagenorhynchus obliquidens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; Delphinidae; Lagenorhynchus
Orthologs
human mouse all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Location:
chromosome: Un
Exon count:
18
Annotation release Status Assembly Chr Location
100 current ASM367639v1 (GCF_003676395.1) Unplaced Scaffold NW_020837964.1 (18438298..18479460, complement)

NW_020837964.1Genomic Context describing neighboring genes Neighboring gene nuclear factor of activated T cells 3 Neighboring gene U6 spliceosomal RNA Neighboring gene transfer RNA alanine (anticodon UGC) Neighboring gene uncharacterized LOC113627172 Neighboring gene DEAD-box helicase 28 Neighboring gene dipeptidase 2

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NW_020837964 Unplaced Scaffold Reference ASM367639v1 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables flavin adenine dinucleotide binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables tRNA binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables tRNA dihydrouridine synthase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in tRNA dihydrouridine synthesis IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs of Annotated Genomes: Lagenorhynchus obliquidens Annotation Release 100 details...Open this link in a new tab

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

Reference ASM367639v1 Primary Assembly

Genomic

  1. NW_020837964.1 Reference ASM367639v1 Primary Assembly

    Range
    18438298..18479460 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_027119509.1 → XP_026975310.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X1

    Related
    ENSLOBP00000004174.1, ENSLOBT00000004678.1
    Conserved Domains (2) summary
    cd02801
    Location:13 → 259
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  2. XM_027119513.1 → XP_026975314.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X5

    Conserved Domains (2) summary
    cd02801
    Location:13 → 214
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:272 → 339
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  3. XM_027119511.1 → XP_026975312.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X3

    Conserved Domains (2) summary
    cd02801
    Location:7 → 211
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:321 → 388
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  4. XM_027119510.1 → XP_026975311.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    Conserved Domains (2) summary
    cd02801
    Location:13 → 237
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:347 → 414
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  5. XM_027119512.1 → XP_026975313.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X4

    Conserved Domains (2) summary
    cd00048
    Location:280 → 344
    DSRM; Double-stranded RNA binding motif. Binding is not sequence specific but is highly specific for double stranded RNA. Found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila staufen protein, E. coli RNase III, ...
    cd02801
    Location:15 → 170
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.