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Database: UniProt
Entry: A0A2Y9PHY1_DELLE
LinkDB: A0A2Y9PHY1_DELLE
Original site: A0A2Y9PHY1_DELLE 
ID   A0A2Y9PHY1_DELLE        Unreviewed;       227 AA.
AC   A0A2Y9PHY1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|RuleBase:RU367024};
DE            Short=dUTPase {ECO:0000256|RuleBase:RU367024};
DE            EC=3.6.1.23 {ECO:0000256|RuleBase:RU367024};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000256|RuleBase:RU367024};
GN   Name=DUT {ECO:0000313|RefSeq:XP_022442882.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022442882.1};
RN   [1] {ECO:0000313|RefSeq:XP_022442882.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022442882.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in nucleotide metabolism via production of dUMP, the
CC       immediate precursor of thymidine nucleotides, and decreases the
CC       intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. {ECO:0000256|RuleBase:RU367024}.
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:0000256|RuleBase:RU367024};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU367024};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2. {ECO:0000256|ARBA:ARBA00005142,
CC       ECO:0000256|RuleBase:RU367024}.
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581, ECO:0000256|RuleBase:RU367024}.
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DR   RefSeq; XP_022442882.1; XM_022587174.1.
DR   AlphaFoldDB; A0A2Y9PHY1; -.
DR   STRING; 9749.A0A2Y9PHY1; -.
DR   InParanoid; A0A2Y9PHY1; -.
DR   OrthoDB; 1343066at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367024};
KW   Magnesium {ECO:0000256|RuleBase:RU367024};
KW   Metal-binding {ECO:0000256|RuleBase:RU367024};
KW   Nucleotide metabolism {ECO:0000256|RuleBase:RU367024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          97..225
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   227 AA;  24958 MW;  2CCF7E0A87154071 CRC64;
     MTYLCPRPVL GYHFLPSLLR SVFNGARQAR PRTEAAGPSW PDLFRGGFPA PNLRPISPLS
     QNRGLVRQEA QIISPSKRAR PAEEGGMRLR FVRLSEHATA PTKGSERAAG YDLYSAYDYT
     VPPMEKALVK TDIQIALPSG CYGRVAPRSG LAAKHFIDVG AGVIDEDYRG NVGVVLFNFG
     KEKFEVKKGD RIAQLICERI FYPEIEEVQV LDDTERGSGG FGSTGNN
//
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