P03195 (DUT_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Short name=dUTPase
EC=3.6.1.23

Alternative name(s):
dUTP pyrophosphatase

Gene names

Name:	DUT
ORF Names:	BLLF3

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into DNA. Induces immune dysregulation that contributes to the pathophysiology of the virus infection.
Catalytic activity	dUTP + H2O = dUMP + diphosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the dUTPase family.
Caution	BLLF3 is known as BLLF2 in Ref.1.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dUTP diphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 278

278

Deoxyuridine 5'-triphosphate nucleotidohydrolase

PRO_0000182962

Regions

Region

171 – 173

3

Substrate binding

Sites

Binding site

76

1

Substrate; via amide nitrogen

Binding site

84

1

Substrate; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Disulfide bond

4 ↔ 246

Secondary structure

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278

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Beta strand

16 – 22

7

Beta strand

25 – 32

8

Beta strand

34 – 36

3

Beta strand

40 – 51

12

Beta strand

56 – 63

8

Beta strand

65 – 70

6

Beta strand

73 – 75

3

Beta strand

83 – 93

11

Beta strand

95 – 97

3

Beta strand

103 – 112

10

Beta strand

127 – 130

4

Beta strand

134 – 137

4

Beta strand

142 – 144

3

Beta strand

149 – 154

6

Beta strand

164 – 169

6

Helix

172 – 176

5

Beta strand

179 – 181

3

Beta strand

190 – 197

8

Beta strand

199 – 201

3

Beta strand

203 – 205

3

Beta strand

210 – 218

9

Helix

219 – 221

3

Beta strand

222 – 224

3

Turn

232 – 235

4

Beta strand

237 – 242

6

Beta strand

248 – 250

3

Helix

252 – 254

3

Sequences

	Sequence		Length	Mass (Da)
	P03195 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 73C90EFF4B863525	FASTA	278	30,953
	10 20 30 40 50 60 MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA RPPEGHGLML 70 80 90 100 110 120 WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS ELKIHLAAFR YATPQMEEDK 130 140 150 160 170 180 GPINHPQYPG DVGLDVSLPK DLALFPHQTV SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL 190 200 210 220 230 240 VKPCRWRRGG VDVSLTNFSD QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL 250 260 270 FRWASCTFEE VPSLAMGDSG LSEALEGRQG RGFGSSGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases." Tarbouriech N., Buisson M., Seigneurin J.M., Cusack S., Burmeister W.P. Structure 13:1299-1310(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4-116 AND 121-256, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01555 Genomic DNA. Translation: CAA24850.1.
AJ507799 Genomic DNA. Translation: CAD53414.1.

PIR

QQBE17. A03758.

RefSeq

YP_401664.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BSY	X-ray	1.50	A	1-278	[»]
2BT1	X-ray	2.70	A	1-278	[»]
2WE0	X-ray	2.01	A	1-278	[»]
2WE1	X-ray	1.80	A	1-278	[»]
2WE2	X-ray	1.50	A	1-278	[»]
2WE3	X-ray	2.00	A	1-256	[»]

ProteinModelPortal

P03195.

SMR

P03195. Positions 3-256.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783715.

Phylogenomic databases

ProtClustDB

PHA3131.

Family and domain databases

InterPro

IPR008180. dUTP_pyroPase.
[Graphical view]

Pfam

PF00692. dUTPase. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P03195.

Entry information

Entry name

DUT_EBVB9

Accession

Primary (citable) accession number: P03195
Secondary accession number(s): Q777F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program