Q07275 (DUT_EBVA8) 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 AG876) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

82830 [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	Inferred from homology

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 By similarity.
Catalytic activity	dUTP + H2O = dUMP + diphosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the dUTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	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_0000182963
Regions
	Region	171 – 173	3	Substrate binding By similarity
Sites
	Binding site	76	1	Substrate; via amide nitrogen By similarity
	Binding site	84	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
Amino acid modifications
	Disulfide bond	4 ↔ 246		By similarity
Experimental info
	Sequence conflict	245	1	S → T in AAA02786. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q07275 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 05073FAB4B863531	FASTA	278	30,892
	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 FRWASCAFEE VPGLAMGDSG LSEALEGRQG RGFGSSGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Epstein-Barr virus candidate vaccine antigen gp340/220 is highly conserved between virus types A and B." Lees J.F., Arrand J.E., Pepper S.V., Stewart J.P., Mackett M., Arrand J.R. Virology 195:578-586(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome of Epstein-Barr virus type 2 strain AG876." Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J. Virology 350:164-170(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07923 Genomic DNA. Translation: AAA02786.1. Sequence problems. DQ279927 Genomic DNA. Translation: ABB89239.1.
RefSeq	YP_001129459.1. NC_009334.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5176172.
Phylogenomic databases
ProtClustDB	PHA3131.
Family and domain databases
InterPro	IPR008180. dUTP_pyroPase. [Graphical view]
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DUT_EBVA8

Accession

Primary (citable) accession number: Q07275
Secondary accession number(s): Q1HVG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 26, 2009
Last modified:	April 3, 2013
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program