ID A0A443RX27_9ACAR Unreviewed; 137 AA.
AC A0A443RX27;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=B4U80_07856 {ECO:0000313|EMBL:RWS19725.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS19725.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS19725.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS19725.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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:RWS19725.1}.
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DR EMBL; NCKV01023278; RWS19725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443RX27; -.
DR STRING; 299467.A0A443RX27; -.
DR EnsemblMetazoa; LDEU012315-RA; LDEU012315-PA; LDEU012315.
DR VEuPathDB; VectorBase:LDEU012315; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000288716; 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:UP000288716}.
FT DOMAIN 15..136
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT NON_TER 137
FT /evidence="ECO:0000313|EMBL:RWS19725.1"
SQ SEQUENCE 137 AA; 15104 MW; 879596673B2B62C9 CRC64;
MSSILKVKLL SDLAMVPTKA TEGSAGFDIF APCDYLVPKN GKILIDTYIA IELPSNCYGR
ISPRSGIAWN ASIHVGGGVI DSDYRGSIHV ILFNFNNVDF LIKRGDRFAQ LICERIETPV
IVVVDELDFT KRNNKGL
//
