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Protein

tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]

Gene

DUS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U16 and U17 in cytoplasmic tRNAs.2 Publications

Catalytic activityi

5,6-dihydrouracil(16) in tRNA + NAD(P)+ = uracil(16) in tRNA + NAD(P)H.
5,6-dihydrouracil(17) in tRNA + NAD(P)+ = uracil(17) in tRNA + NAD(P)H.

Cofactori

FMNBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92FMNBy similarity1
Active sitei121Proton donorBy similarity1
Binding sitei160FMNBy similarity1
Binding sitei188FMNBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 37FMNBy similarity3
Nucleotide bindingi223 – 225FMNBy similarity3
Nucleotide bindingi247 – 248FMNBy similarity2

GO - Molecular functioni

GO - Biological processi

  • tRNA modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Flavoprotein, FMN, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32671-MONOMER.
YEAST:G3O-32671-MONOMER.
BRENDAi1.3.1.88. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] (EC:1.3.1.88)
Alternative name(s):
tRNA-dihydrouridine synthase 1
Gene namesi
Name:DUS1
Ordered Locus Names:YML080W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML080W.
SGDiS000004545. DUS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001621532 – 423tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]Add BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP53759.
PRIDEiP53759.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-27885,EBI-16219

Protein-protein interaction databases

BioGridi35061. 20 interactors.
IntActiP53759. 3 interactors.
MINTiMINT-4083769.

Structurei

3D structure databases

ProteinModelPortaliP53759.
SMRiP53759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Dus family. Dus1 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075089.
HOGENOMiHOG000203649.
InParanoidiP53759.
KOiK05542.
OMAiACKGAGA.
OrthoDBiEOG092C1H8A.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEPALSSAN NALMQKLTGR QLFDKIGRPT RIVAPMVDQS ELAWRILSRR
60 70 80 90 100
YGATLAYTPM LHAKLFATSK KYREDNWSSL DGSSVDRPLV VQFCANDPEY
110 120 130 140 150
LLAAAKLVED KCDAVDLNLG CPQGIAKKGH YGSFLMEEWD LIHNLINTLH
160 170 180 190 200
KNLKVPVTAK IRIFDDCEKS LNYAKMVLDA GAQFLTVHGR VREQKGQKTG
210 220 230 240 250
LANWETIKYL RDNLPKETVF FANGNILYPE DISRCMEHIG ADAVMSAEGN
260 270 280 290 300
LYNPGVFNVG QTKNKEKIFP RVDKIIREYF QIVKECQESK ASKTAMKSHF
310 320 330 340 350
FKILRPFLPH HTDIRSTLAT MNAKATWEEW EEQVVKPVEK VVQEIFEQPD
360 370 380 390 400
IAIKDEITIG EKQSWGGSYR TVPYWRCQPY FRPVNGITGD KRVMQGLIDE
410 420
SVNKKRKADV PLESADKKKD VKA
Length:423
Mass (Da):48,131
Last modified:October 1, 1996 - v1
Checksum:i7D226E166CE42F43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46373 Genomic DNA. Translation: CAA86498.1.
BK006946 Genomic DNA. Translation: DAA09817.1.
PIRiS48817.
RefSeqiNP_013631.1. NM_001182439.1.

Genome annotation databases

EnsemblFungiiYML080W; YML080W; YML080W.
GeneIDi854895.
KEGGisce:YML080W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46373 Genomic DNA. Translation: CAA86498.1.
BK006946 Genomic DNA. Translation: DAA09817.1.
PIRiS48817.
RefSeqiNP_013631.1. NM_001182439.1.

3D structure databases

ProteinModelPortaliP53759.
SMRiP53759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35061. 20 interactors.
IntActiP53759. 3 interactors.
MINTiMINT-4083769.

Proteomic databases

MaxQBiP53759.
PRIDEiP53759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML080W; YML080W; YML080W.
GeneIDi854895.
KEGGisce:YML080W.

Organism-specific databases

EuPathDBiFungiDB:YML080W.
SGDiS000004545. DUS1.

Phylogenomic databases

GeneTreeiENSGT00550000075089.
HOGENOMiHOG000203649.
InParanoidiP53759.
KOiK05542.
OMAiACKGAGA.
OrthoDBiEOG092C1H8A.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32671-MONOMER.
YEAST:G3O-32671-MONOMER.
BRENDAi1.3.1.88. 984.

Miscellaneous databases

PROiP53759.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUS1_YEAST
AccessioniPrimary (citable) accession number: P53759
Secondary accession number(s): D6W0K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.