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Database: UniProt
Entry: A0A2P5AVH9_PARAD
LinkDB: A0A2P5AVH9_PARAD
Original site: A0A2P5AVH9_PARAD 
ID   A0A2P5AVH9_PARAD        Unreviewed;       180 AA.
AC   A0A2P5AVH9;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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};
DE   Flags: Fragment;
GN   ORFNames=PanWU01x14_297230 {ECO:0000313|EMBL:PON40481.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON40481.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PON40481.1}.
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DR   EMBL; JXTB01000437; PON40481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5AVH9; -.
DR   STRING; 3476.A0A2P5AVH9; -.
DR   OrthoDB; 1343066at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000237105; 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:UP000237105}.
FT   DOMAIN          51..179
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PON40481.1"
SQ   SEQUENCE   180 AA;  18914 MW;  08F2AD3896950411 CRC64;
     NLPHLLLRMA TNNSPEIKEP ATKLPKLHEN GVGGVSQGSV SFFRVKKLSQ NAVVPSRGSP
     LSAGYDLSSA TETKVPARGK ALVPTDLSIA VPEGTYARIA PRSGLAWKRS IDVGAGVIDA
     DYRGPVGVVL FNHSDVDFEV KAGDRIAQLI IEKIITPDVV EVEDLDATVR GSGGFGSTGV
//
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