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Protein

tRNA-dihydrouridine(20/20a) synthase

Gene

dus

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631FMNCombined sources1 Publication
Sitei90 – 901Interacts with tRNA1 Publication
Active sitei93 – 931Proton donor1 Publication
Sitei97 – 971Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication
Binding sitei132 – 1321FMNCombined sources1 Publication
Binding sitei164 – 1641FMNCombined sources1 Publication
Sitei175 – 1751Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication
Sitei178 – 1781Interacts with tRNA1 Publication
Sitei290 – 2901Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication
Sitei293 – 2931Interacts with tRNA; defines subfamily-specific binding signature1 Publication1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 123FMNCombined sources1 Publication
Nucleotide bindingi203 – 2053FMNCombined sources1 Publication
Nucleotide bindingi225 – 2262FMNCombined sources1 Publication

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • FMN binding Source: UniProtKB
  • tRNA binding Source: UniProtKB
  • 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

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-19-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342tRNA-dihydrouridine(20/20a) synthasePRO_0000433569Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0016.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni12 – 143Combined sources
Helixi17 – 2610Combined sources
Beta strandi28 – 336Combined sources
Helixi39 – 446Combined sources
Helixi47 – 515Combined sources
Helixi55 – 573Combined sources
Beta strandi59 – 657Combined sources
Helixi69 – 8113Combined sources
Beta strandi85 – 917Combined sources
Helixi96 – 1005Combined sources
Helixi104 – 1096Combined sources
Helixi111 – 12414Combined sources
Beta strandi129 – 1357Combined sources
Helixi143 – 15513Combined sources
Beta strandi160 – 1645Combined sources
Helixi176 – 1783Combined sources
Helixi185 – 19410Combined sources
Beta strandi198 – 2058Combined sources
Helixi209 – 2168Combined sources
Beta strandi219 – 2246Combined sources
Helixi226 – 2305Combined sources
Helixi232 – 2354Combined sources
Helixi238 – 2414Combined sources
Helixi251 – 26818Combined sources
Helixi272 – 2765Combined sources
Turni280 – 2856Combined sources
Helixi289 – 29911Combined sources
Helixi302 – 31615Combined sources

3D structure databases

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

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-19-MONOMER.

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: September 7, 2016
This is version 76 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.