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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into viral DNA.UniRule annotation

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76Substrate; via amide nitrogen1
Binding sitei84Substrate; via amide nitrogen and carbonyl oxygen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.1.23. 2112.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolaseUniRule annotation (EC:3.6.1.23UniRule annotation)
Short name:
dUTPaseUniRule annotation
Alternative name(s):
dUTP pyrophosphataseUniRule annotation
Gene namesi
Name:DUTUniRule annotation
ORF Names:BLLF3
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001829621 – 278Deoxyuridine 5'-triphosphate nucleotidohydrolaseAdd BLAST278

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi4 ↔ 246

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP03195. 5 interactors.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi16 – 22Combined sources7
Beta strandi25 – 32Combined sources8
Beta strandi34 – 36Combined sources3
Beta strandi40 – 51Combined sources12
Beta strandi56 – 63Combined sources8
Beta strandi65 – 70Combined sources6
Beta strandi73 – 75Combined sources3
Beta strandi83 – 93Combined sources11
Beta strandi95 – 97Combined sources3
Beta strandi103 – 112Combined sources10
Beta strandi127 – 130Combined sources4
Beta strandi134 – 137Combined sources4
Beta strandi142 – 144Combined sources3
Beta strandi149 – 154Combined sources6
Beta strandi164 – 169Combined sources6
Helixi172 – 176Combined sources5
Beta strandi179 – 181Combined sources3
Beta strandi190 – 197Combined sources8
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi210 – 218Combined sources9
Helixi219 – 221Combined sources3
Beta strandi222 – 224Combined sources3
Turni232 – 235Combined sources4
Beta strandi237 – 242Combined sources6
Beta strandi248 – 250Combined sources3
Helixi252 – 254Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BSYX-ray1.50A1-278[»]
2BT1X-ray2.70A1-278[»]
2WE0X-ray2.01A1-278[»]
2WE1X-ray1.80A1-278[»]
2WE2X-ray1.50A1-278[»]
2WE3X-ray2.00A1-256[»]
ProteinModelPortaliP03195.
SMRiP03195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03195.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni171 – 173Substrate bindingUniRule annotation3
Regioni273 – 274Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

Family and domain databases

CDDicd07557. trimeric_dUTPase. 2 hits.
Gene3Di2.70.40.10. 3 hits.
HAMAPiMF_04031. HSV_DUT. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 2 hits.

Sequencei

Sequence statusi: Complete.

P03195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA
60 70 80 90 100
RPPEGHGLML WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS
110 120 130 140 150
ELKIHLAAFR YATPQMEEDK GPINHPQYPG DVGLDVSLPK DLALFPHQTV
160 170 180 190 200
SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL VKPCRWRRGG VDVSLTNFSD
210 220 230 240 250
QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL FRWASCTFEE
260 270
VPSLAMGDSG LSEALEGRQG RGFGSSGQ
Length:278
Mass (Da):30,953
Last modified:July 21, 1986 - v1
Checksum:i73C90EFF4B863525
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24850.1.
AJ507799 Genomic DNA. Translation: CAD53414.1.
PIRiA03758. QQBE17.
RefSeqiYP_401664.1. NC_007605.1.

Genome annotation databases

GeneIDi3783715.
KEGGivg:3783715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24850.1.
AJ507799 Genomic DNA. Translation: CAD53414.1.
PIRiA03758. QQBE17.
RefSeqiYP_401664.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BSYX-ray1.50A1-278[»]
2BT1X-ray2.70A1-278[»]
2WE0X-ray2.01A1-278[»]
2WE1X-ray1.80A1-278[»]
2WE2X-ray1.50A1-278[»]
2WE3X-ray2.00A1-256[»]
ProteinModelPortaliP03195.
SMRiP03195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03195. 5 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783715.
KEGGivg:3783715.

Enzyme and pathway databases

BRENDAi3.6.1.23. 2112.

Miscellaneous databases

EvolutionaryTraceiP03195.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 2 hits.
Gene3Di2.70.40.10. 3 hits.
HAMAPiMF_04031. HSV_DUT. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDUT_EBVB9
AccessioniPrimary (citable) accession number: P03195
Secondary accession number(s): Q777F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

BLLF3 is known as BLLF2 in PubMed:6087149.Curated

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.