Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA-dihydrouridine(20/20a) synthase

Gene

dus

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.UniRule annotation2 Publications

Catalytic activityi

5,6-dihydrouracil(20) in tRNA + NAD(P)+ = uracil(20) in tRNA + NAD(P)H.UniRule annotation
5,6-dihydrouracil(20a) in tRNA + NAD(P)+ = uracil(20a) in tRNA + NAD(P)H.UniRule annotation

Cofactori

FMNUniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63FMNCombined sources1 Publication1
Sitei90Interacts with tRNA1 Publication1
Active sitei93Proton donor1 Publication1
Sitei97Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication1
Binding sitei132FMNCombined sources1 Publication1
Binding sitei164FMNCombined sources1 Publication1
Sitei175Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication1
Sitei178Interacts with tRNA1 Publication1
Sitei290Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication1
Sitei293Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 12FMNCombined sources1 Publication3
Nucleotide bindingi203 – 205FMNCombined sources1 Publication3
Nucleotide bindingi225 – 226FMNCombined sources1 Publication2

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • FMN binding Source: UniProtKB
  • tRNA binding Source: UniProtKB
  • tRNA-dihydrouridine20 synthase activity Source: UniProtKB-EC
  • tRNA dihydrouridine synthase activity Source: UniProtKB

GO - Biological processi

  • tRNA dihydrouridine synthesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Flavoprotein, FMN, NADP, Nucleotide-binding, RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(20/20a) synthaseUniRule annotation1 Publication (EC:1.3.1.-UniRule annotationBy similarity, EC:1.3.1.91UniRule annotationBy similarity)
Alternative name(s):
DusA-like U20-specific dihydrouridine synthase1 PublicationUniRule annotation
Short name:
U20-specific Dus1 PublicationUniRule annotation
Gene namesi
Name:dus
Ordered Locus Names:TTHA0016Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004335691 – 342tRNA-dihydrouridine(20/20a) synthaseAdd BLAST342

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0016.

Structurei

Secondary structure

1342
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni12 – 14Combined sources3
Helixi17 – 26Combined sources10
Beta strandi28 – 33Combined sources6
Helixi39 – 44Combined sources6
Helixi47 – 51Combined sources5
Helixi55 – 57Combined sources3
Beta strandi59 – 65Combined sources7
Helixi69 – 81Combined sources13
Beta strandi85 – 91Combined sources7
Helixi96 – 100Combined sources5
Helixi104 – 109Combined sources6
Helixi111 – 124Combined sources14
Beta strandi129 – 135Combined sources7
Helixi143 – 155Combined sources13
Beta strandi160 – 164Combined sources5
Helixi176 – 178Combined sources3
Helixi185 – 194Combined sources10
Beta strandi198 – 205Combined sources8
Helixi209 – 216Combined sources8
Beta strandi219 – 224Combined sources6
Helixi226 – 230Combined sources5
Helixi232 – 235Combined sources4
Helixi238 – 241Combined sources4
Helixi251 – 268Combined sources18
Helixi272 – 276Combined sources5
Turni280 – 285Combined sources6
Helixi289 – 299Combined sources11
Helixi302 – 316Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B0PX-ray1.70A/B1-342[»]
3B0UX-ray1.95X/Y1-342[»]
3B0VX-ray3.51C/D1-342[»]
ProteinModelPortaliQ5SMC7.
SMRiQ5SMC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Dus family. DusA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000259834.
KOiK05539.
OMAiEQDSYEF.
PhylomeDBiQ5SMC7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02041. DusA_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004653. DusA.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SMC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDPRLSVAP MVDRTDRHFR FLVRQVSLGV RLYTEMTVDQ AVLRGNRERL
60 70 80 90 100
LAFRPEEHPI ALQLAGSDPK SLAEAARIGE AFGYDEINLN LGCPSEKAQE
110 120 130 140 150
GGYGACLLLD LARVREILKA MGEAVRVPVT VKMRLGLEGK ETYRGLAQSV
160 170 180 190 200
EAMAEAGVKV FVVHARSALL ALSTKANREI PPLRHDWVHR LKGDFPQLTF
210 220 230 240 250
VTNGGIRSLE EALFHLKRVD GVMLGRAVYE DPFVLEEADR RVFGLPRRPS
260 270 280 290 300
RLEVARRMRA YLEEEVLKGT PPWAVLRHML NLFRGRPKGR LWRRLLSEGR
310 320 330 340
SLQALDRALR LMEEEVGEEG EKEKPGPRGQ REAAPGPARE GV
Length:342
Mass (Da):38,474
Last modified:December 21, 2004 - v1
Checksum:i19DB0828A4C994E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69839.1.
RefSeqiWP_011227643.1. NC_006461.1.
YP_143282.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69839; BAD69839; BAD69839.
GeneIDi3168530.
KEGGittj:TTHA0016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69839.1.
RefSeqiWP_011227643.1. NC_006461.1.
YP_143282.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B0PX-ray1.70A/B1-342[»]
3B0UX-ray1.95X/Y1-342[»]
3B0VX-ray3.51C/D1-342[»]
ProteinModelPortaliQ5SMC7.
SMRiQ5SMC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD69839; BAD69839; BAD69839.
GeneIDi3168530.
KEGGittj:TTHA0016.

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000259834.
KOiK05539.
OMAiEQDSYEF.
PhylomeDBiQ5SMC7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02041. DusA_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004653. DusA.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUSAL_THET8
AccessioniPrimary (citable) accession number: Q5SMC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: December 21, 2004
Last modified: November 30, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.