ID DUT_EBVB9 Reviewed; 278 AA. AC P03195; Q777F3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 105. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031}; DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031}; DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031}; GN Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; ORFNames=BLLF3; OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Lymphocryptovirus; OC Lymphocryptovirus humangamma4; Epstein-Barr virus (strain GD1). OX NCBI_TaxID=10377; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=6087149; DOI=10.1038/310207a0; RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., RA Tuffnell P.S., Barrell B.G.; RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome."; RL Nature 310:207-211(1984). RN [2] RP GENOME REANNOTATION. RX PubMed=12771413; DOI=10.1099/vir.0.19054-0; RA de Jesus O., Smith P.R., Spender L.C., Elgueta Karstegl C., Niller H.H., RA Huang D., Farrell P.J.; RT "Updated Epstein-Barr virus (EBV) DNA sequence and analysis of a promoter RT for the BART (CST, BARF0) RNAs of EBV."; RL Virology 84:1443-1450(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4-116 AND 121-256, AND SUBUNIT. RX PubMed=16154087; DOI=10.1016/j.str.2005.06.009; RA Tarbouriech N., Buisson M., Seigneurin J.M., Cusack S., Burmeister W.P.; RT "The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases."; RL Structure 13:1299-1310(2005). CC -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the CC immediate precursor of thymidine nucleotides and decreases the CC intracellular concentration of dUTP to avoid uracil incorporation into CC viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; CC Evidence={ECO:0000255|HAMAP-Rule:MF_04031}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04031}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16154087}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP- CC Rule:MF_04031}. CC -!- CAUTION: BLLF3 is known as BLLF2 in PubMed:6087149. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V01555; CAA24850.1; -; Genomic_DNA. DR EMBL; AJ507799; CAD53414.1; -; Genomic_DNA. DR PIR; A03758; QQBE17. DR RefSeq; YP_401664.1; NC_007605.1. DR PDB; 2BSY; X-ray; 1.50 A; A=1-278. DR PDB; 2BT1; X-ray; 2.70 A; A=1-278. DR PDB; 2WE0; X-ray; 2.01 A; A=1-278. DR PDB; 2WE1; X-ray; 1.80 A; A=1-278. DR PDB; 2WE2; X-ray; 1.50 A; A=1-278. DR PDB; 2WE3; X-ray; 2.00 A; A=1-256. DR PDBsum; 2BSY; -. DR PDBsum; 2BT1; -. DR PDBsum; 2WE0; -. DR PDBsum; 2WE1; -. DR PDBsum; 2WE2; -. DR PDBsum; 2WE3; -. DR SMR; P03195; -. DR IntAct; P03195; 5. DR MINT; P03195; -. DR DNASU; 3783715; -. DR GeneID; 3783715; -. DR KEGG; vg:3783715; -. DR BRENDA; 3.6.1.23; 2112. DR EvolutionaryTrace; P03195; -. DR Proteomes; UP000153037; Segment. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07557; trimeric_dUTPase; 2. DR Gene3D; 2.70.40.10; -; 2. DR HAMAP; MF_04031; HSV_DUT; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR036157; dUTPase-like_sf. DR InterPro; IPR033704; dUTPase_trimeric. DR InterPro; IPR034745; HSV_DUT. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; dUTPase-like; 2. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Hydrolase; Magnesium; Metal-binding; KW Nucleotide metabolism; Reference proteome. FT CHAIN 1..278 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182962" FT BINDING 76 FT /ligand="substrate" FT BINDING 84 FT /ligand="substrate" FT BINDING 171..173 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04031" FT BINDING 273..274 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04031" FT DISULFID 4..246 FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 16..22 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 25..32 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 40..51 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 83..93 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:2WE2" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:2BSY" FT HELIX 172..176 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 190..197 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:2BSY" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:2BSY" FT TURN 232..235 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:2BSY" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:2BSY" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:2BSY" SQ SEQUENCE 278 AA; 30953 MW; 73C90EFF4B863525 CRC64; MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA RPPEGHGLML WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS ELKIHLAAFR YATPQMEEDK GPINHPQYPG DVGLDVSLPK DLALFPHQTV SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL VKPCRWRRGG VDVSLTNFSD QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL FRWASCTFEE VPSLAMGDSG LSEALEGRQG RGFGSSGQ //