DUS1L dihydrouridine synthase 1 like [Canis lupus familiaris (dog)] - Gene

Summary

Official Symbol: DUS1Lprovided by VGNC
Official Full Name: dihydrouridine synthase 1 likeprovided by VGNC
Primary source: VGNC:VGNC:53235
See related: Ensembl:ENSCAFG00845007773
Gene type: protein coding
RefSeq status: MODEL
Organism: Canis lupus familiaris (sub-species: familiaris)
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 9

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
106	current	ROS_Cfam_1.0 (GCF_014441545.1)	9	NC_051813.1 (850263..855675)
106	current	Dog10K_Boxer_Tasha (GCF_000002285.5)	9	NC_006591.4 (858814..864224)
106	current	UU_Cfam_GSD_1.0 (GCF_011100685.1)	9	NC_049230.1 (1080645..1086055)
106	current	UMICH_Zoey_3.1 (GCF_005444595.1)	9	NC_049269.1 (875208..880618)
106	current	UNSW_CanFamBas_1.0 (GCF_013276365.1)	9	NC_049750.1 (1002124..1007532)

Chromosome 9 - NC_051813.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables flavin adenine dinucleotide 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 processing	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like

XP_005624033.1

EC 1.3.1.88

XP_005624035.1

EC 1.3.1.88

XP_005624037.1

EC 1.3.1.88

XP_005624038.1

EC 1.3.1.88

XP_005624039.1

EC 1.3.1.88

XP_038340549.1

EC 1.3.1.88

XP_038340550.1

EC 1.3.1.88

XP_038340551.1

EC 1.3.1.88

XP_038340552.1

EC 1.3.1.88

XP_038340553.1

EC 1.3.1.88

XP_038340554.1

EC 1.3.1.88

XP_038340555.1

EC 1.3.1.88

XP_038402191.1

EC 1.3.1.88

XP_038402192.1

EC 1.3.1.88

XP_038402193.1

EC 1.3.1.88

XP_038402194.1

EC 1.3.1.88

XP_038402195.1

EC 1.3.1.88

XP_038402196.1

EC 1.3.1.88

XP_038402197.1

EC 1.3.1.88

XP_038466198.1

EC 1.3.1.88

XP_038466199.1

EC 1.3.1.88

XP_038466200.1

EC 1.3.1.88

XP_038466201.1

EC 1.3.1.88

XP_038466202.1

EC 1.3.1.88

XP_038466203.1

EC 1.3.1.88

XP_038466204.1

EC 1.3.1.88

XP_038478979.1

EC 1.3.1.88

XP_038531308.1

EC 1.3.1.88

XP_038531309.1

EC 1.3.1.88

XP_038531310.1

EC 1.3.1.88

XP_038531311.1

EC 1.3.1.88

XP_038531312.1

EC 1.3.1.88

XP_038531314.1

EC 1.3.1.88

XP_038531315.1

EC 1.3.1.88

XP_848227.1

EC 1.3.1.88

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Canis lupus familiaris Annotation Release 106 details...

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

Reference ROS_Cfam_1.0

Genomic

NC_051813.1 Reference ROS_Cfam_1.0

Range

850263..855675

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_038675380.1 → XP_038531308.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038675383.1 → XP_038531311.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3

UniProtKB/TrEMBL

A0A8C0K8G6

Conserved Domains (1) summary

cd02801
Location:18 → 250

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 ...
XM_038675384.1 → XP_038531312.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4

UniProtKB/TrEMBL

A0A8C0Q9N1, A0A8C0QAT4

Conserved Domains (2) summary

TIGR01623
Location:438 → 471

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038675382.1 → XP_038531310.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (2) summary

TIGR01623
Location:438 → 473

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038675386.1 → XP_038531314.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5

UniProtKB/TrEMBL

A0A8C0K8G6, A0A8C0RN40, A0A8I3N962

Related

ENSCAFP00845010626.1, ENSCAFT00845013689.1

Conserved Domains (2) summary

TIGR01623
Location:396 → 431

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 250

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 ...
XM_038675387.1 → XP_038531315.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038675381.1 → XP_038531309.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...

Alternate UMICH_Zoey_3.1

Genomic

NC_049269.1 Alternate UMICH_Zoey_3.1

Range

875208..880618

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_038484621.1 → XP_038340549.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038484624.1 → XP_038340552.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3

Conserved Domains (1) summary

cd02801
Location:18 → 250

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 ...
XM_038484625.1 → XP_038340553.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4

Conserved Domains (2) summary

TIGR01623
Location:438 → 471

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038484623.1 → XP_038340551.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2

Conserved Domains (2) summary

TIGR01623
Location:438 → 473

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038484626.1 → XP_038340554.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5

Conserved Domains (2) summary

TIGR01623
Location:396 → 431

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 250

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 ...
XM_038484627.1 → XP_038340555.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038484622.1 → XP_038340550.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...

Alternate UNSW_CanFamBas_1.0

Genomic

NC_049750.1 Alternate UNSW_CanFamBas_1.0

Range

1002124..1007532

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_038610270.1 → XP_038466198.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038610273.1 → XP_038466201.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3

Conserved Domains (1) summary

cd02801
Location:18 → 250

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 ...
XM_038610274.1 → XP_038466202.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4

Conserved Domains (2) summary

TIGR01623
Location:438 → 471

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038610272.1 → XP_038466200.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2

Conserved Domains (2) summary

TIGR01623
Location:438 → 473

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_038610275.1 → XP_038466203.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5

Conserved Domains (2) summary

TIGR01623
Location:396 → 431

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 250

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 ...
XM_038610276.1 → XP_038466204.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038610271.1 → XP_038466199.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...

Alternate UU_Cfam_GSD_1.0

Genomic

NC_049230.1 Alternate UU_Cfam_GSD_1.0

Range

1080645..1086055

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_038546263.1 → XP_038402191.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

UniProtKB/TrEMBL

A0A8C0QAT4
XM_038546266.1 → XP_038402194.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3

UniProtKB/TrEMBL

A0A8C0K8G6
XM_038546267.1 → XP_038402195.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4

UniProtKB/TrEMBL

A0A8C0QAT4
XM_038546265.1 → XP_038402193.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2

UniProtKB/TrEMBL

A0A8C0QAT4
XM_038546268.1 → XP_038402196.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5

UniProtKB/TrEMBL

A0A8C0K8G6
XM_038546269.1 → XP_038402197.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6

UniProtKB/TrEMBL

A0A8C0QAT4
XM_038546264.1 → XP_038402192.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

UniProtKB/TrEMBL

A0A8C0QAT4

Alternate Dog10K_Boxer_Tasha Primary Assembly

Genomic

NC_006591.4 Alternate Dog10K_Boxer_Tasha Primary Assembly

Range

858814..864224

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_005623976.4 → XP_005624033.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

See identical proteins and their annotated locations for XP_005624033.1

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_005623980.4 → XP_005624037.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3

UniProtKB/TrEMBL

A0A8C0K8G6

Conserved Domains (1) summary

cd02801
Location:18 → 250

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 ...
XM_005623981.4 → XP_005624038.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4

UniProtKB/TrEMBL

A0A8C0Q9N1, A0A8C0QAT4

Conserved Domains (2) summary

TIGR01623
Location:438 → 471

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_005623978.4 → XP_005624035.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (2) summary

TIGR01623
Location:438 → 473

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 292

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 ...
XM_843134.6 → XP_848227.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5

UniProtKB/TrEMBL

A0A8C0K8G6, A0A8C0RN40, A0A8I3N962

Conserved Domains (2) summary

TIGR01623
Location:396 → 431

put_zinc_LRP1; putative zinc finger domain, LRP1 type

cd02801
Location:18 → 250

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 ...
XM_005623982.4 → XP_005624039.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...
XM_038623051.1 → XP_038478979.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1

UniProtKB/TrEMBL

A0A8C0QAT4

Conserved Domains (1) summary

cd02801
Location:18 → 292

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 ...