GenomeNet

Database: UniProt
Entry: G3WIR7_SARHA
LinkDB: G3WIR7_SARHA
Original site: G3WIR7_SARHA 
ID   G3WIR7_SARHA            Unreviewed;       198 AA.
AC   G3WIR7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:ENSSHAP00000015322.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000015322.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000015322.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000015322.1}
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   AlphaFoldDB; G3WIR7; -.
DR   STRING; 9305.ENSSHAP00000015322; -.
DR   Ensembl; ENSSHAT00000015449.2; ENSSHAP00000015322.1; ENSSHAG00000013061.2.
DR   eggNOG; KOG3370; Eukaryota.
DR   GeneTree; ENSGT00390000018390; -.
DR   HOGENOM; CLU_068508_2_1_1; -.
DR   OMA; ICYPDLE; -.
DR   TreeFam; TF105416; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000007648; 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:UP000007648}.
FT   DOMAIN          68..196
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  21266 MW;  DE568B30A3339345 CRC64;
     MGAVSRACRT TSRRGPLGRP SALLHASHRE MPCSEAVPAG VSPSKRARPA EQEPEGPVRL
     RFARLSEHAT APSKGSARAA GYDLYSAYDY TIPAMEKALV KTDIQISLPP GCYGRVAPRS
     GLAAKHFIDV GAGVIDEDYR GNVGVVLFNF GKETFEVKKG DRIAQLICER VFYPELEEVQ
     GLDDTERGAG GFGSTGQN
//
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