ID   I3MAG5_ICTTR            Unreviewed;       164 AA.
AC   I3MAG5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 54.
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|Ensembl:ENSSTOP00000006989.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000006989.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000006989.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AGTP01002560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MAG5; -.
DR   STRING; 43179.ENSSTOP00000006989; -.
DR   Ensembl; ENSSTOT00000007806.3; ENSSTOP00000006989.3; ENSSTOG00000007811.3.
DR   eggNOG; KOG3370; Eukaryota.
DR   GeneTree; ENSGT00390000018390; -.
DR   HOGENOM; CLU_068508_2_0_1; -.
DR   InParanoid; I3MAG5; -.
DR   TreeFam; TF105416; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
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:UP000005215}.
FT   DOMAIN          34..162
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   164 AA;  17867 MW;  DFE74948BE939721 CRC64;
     MPSSEEVTAI SPSKRARPAE DGGLRLRFVR LSEHATAPTR GSARAAGYDL YSAYDYIVPP
     MEKALVKTDI QIALPSGCYG RIAPRSGLAA KYFIDVGAGV IDEDYRGNIG VVLFNFGKEK
     FEVKKGDRIA QLICERIFYP DIEEVQVLND TERGSGGFGS TGKN
//