NEW
Try the new Transcript table
The following sections contain reference sequences that belong to a
specific genome build. Explain
This section includes genomic Reference
Sequences (RefSeqs) from all assemblies on which this gene is annotated, such as
RefSeqs for chromosomes and scaffolds (contigs) from both reference and alternate
assemblies. Model RNAs and proteins are also reported here.
Reference Pvam_2.0
Genomic
-
NW_011889008.1 Reference Pvam_2.0
- Range
-
737815..747304
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
XM_023538620.1 → XP_023394388.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X4
- UniProtKB/TrEMBL
-
A0A6P6D422
- Conserved Domains (2) summary
-
- cd02801
Location:23 → 283
- 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 ...
- cl27070
Location:429 → 464
- DUF702; Domain of unknown function (DUF702)
-
XM_023538616.1 → XP_023394384.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X1
- UniProtKB/TrEMBL
-
A0A6P6D3U0
- Conserved Domains (2) summary
-
- cd02801
Location:45 → 305
- 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 ...
- cl27070
Location:451 → 486
- DUF702; Domain of unknown function (DUF702)
-
XM_023538619.1 → XP_023394387.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X3
- UniProtKB/TrEMBL
-
A0A6P6D4B8
- Conserved Domains (2) summary
-
- cd02801
Location:45 → 266
- 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 ...
- cl27070
Location:412 → 447
- DUF702; Domain of unknown function (DUF702)
-
XM_023538621.1 → XP_023394389.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5
- UniProtKB/TrEMBL
-
A0A6P3QXB6
- Conserved Domains (1) summary
-
- cd02801
Location:18 → 278
- 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_011373664.1 → XP_011371966.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5
See identical proteins and their annotated locations for XP_011371966.1
- UniProtKB/TrEMBL
-
A0A6P3QXB6
- Conserved Domains (1) summary
-
- cd02801
Location:18 → 278
- 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_011373665.1 → XP_011371967.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X5
See identical proteins and their annotated locations for XP_011371967.1
- UniProtKB/TrEMBL
-
A0A6P3QXB6
- Conserved Domains (1) summary
-
- cd02801
Location:18 → 278
- 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_023538617.1 → XP_023394385.1 tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X2
- UniProtKB/TrEMBL
-
A0A6P6D592
- 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 ...