ID DUT_FOWPN Reviewed; 145 AA. AC Q9J5G5; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 08-NOV-2023, entry version 83. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase; DE Short=dUTPase; DE EC=3.6.1.23; DE AltName: Full=dUTP pyrophosphatase; GN Name=DUT; OrderedLocusNames=FPV038; OS Fowlpox virus (strain NVSL) (FPV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus; Fowlpox virus. OX NCBI_TaxID=928301; OH NCBI_TaxID=7742; Vertebrata. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000; RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.; RT "The genome of fowlpox virus."; RL J. Virol. 74:3815-3831(2000). CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces CC dUMP, the immediate precursor of thymidine nucleotides and it decreases CC the intracellular concentration of dUTP so that uracil cannot be CC incorporated into DNA. {ECO:0000250}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the dUTPase family. {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; AF198100; AAF44382.1; -; Genomic_DNA. DR RefSeq; NP_039001.1; NC_002188.1. DR SMR; Q9J5G5; -. DR GeneID; 1486586; -. DR KEGG; vg:1486586; -. DR Proteomes; UP000008597; Segment. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro. DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 1. DR InterPro; IPR008181; dUTPase. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR036157; dUTPase-like_sf. DR InterPro; IPR033704; dUTPase_trimeric. DR NCBIfam; TIGR00576; dut; 1. DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1. DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Reference proteome. FT CHAIN 1..145 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182947" SQ SEQUENCE 145 AA; 16253 MW; 94CF5F6963B47D08 CRC64; MEEVTVYKIS DRAKLPYKQT SYSAGYDLYS AYDYVIEPMN KELIKTDIIL KIPNGYYGRI APRSGLAYNY FIDVGAGVID SDYRGNVGVL LFNFGSTQFN VCKGDRIAQI IFEKIAYPKI IEVTTLEEIN ITDRGNSGFG STGLK //