ID D3TSN9_GLOMM Unreviewed; 182 AA.
AC D3TSN9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 36.
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};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD20717.1};
RN [1] {ECO:0000313|EMBL:ADD20717.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20717.1};
RX PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT "An insight into the sialome of Glossina morsitans morsitans.";
RL BMC Genomics 11:213-213(2010).
RN [2] {ECO:0000313|EMBL:ADD20717.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20717.1};
RG International Glossina Genome Initiative;
RA da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., Haines L.R.,
RA Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RL Submitted (JAN-2010) 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}.
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DR EMBL; EZ424441; ADD20717.1; -; mRNA.
DR AlphaFoldDB; D3TSN9; -.
DR UniPathway; UPA00610; UER00666.
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 2: Evidence at transcript level;
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}.
FT DOMAIN 34..158
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 145..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 19907 MW; A8626319B583FA15 CRC64;
MLAEGEVEPV AKKMKLDTKC VLCWAKLTEH ALEPVRGSER AAGLDLRSAY DLKVPARGKA
LVKTDLQIQV PSGSYGRVAP RSGLAWKNFI DVGAGVIDED YRGNLGVLLF NHSDVDFDVK
RGDRIAQLIC ERIFYPELEQ VDKLEDTQRG EGGFGSTGVT DLPAADKNGE CKAEKEKEVA
KS
//
