ID   DUT_SIRV1               Reviewed;         158 AA.
AC   O71028; Q5TJA2; Q777W3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-NOV-2023, entry version 95.
DE   RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   ORFNames=158a;
OS   Sulfolobus islandicus rod-shaped virus 1 (SIRV-1) (Sulfolobus virus
OS   SIRV-1).
OC   Viruses; Adnaviria; Zilligvirae; Taleaviricota; Tokiviricetes;
OC   Ligamenvirales; Rudiviridae; Icerudivirus; Icerudivirus SIRV1.
OX   NCBI_TaxID=157898;
OH   NCBI_TaxID=43080; Sulfolobus islandicus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND ENZYME ACTIVITY.
RX   PubMed=9497317; DOI=10.1074/jbc.273.11.6024;
RA   Prangishvili D., Klenk H.-P., Jakobs G., Schmiechen A., Hanselmann C.,
RA   Holz I., Zillig W.;
RT   "Biochemical and phylogenetic characterization of the dUTPase from the
RT   archaeal virus SIRV.";
RL   J. Biol. Chem. 273:6024-6029(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate variant VIII;
RX   PubMed=11878892; DOI=10.1006/viro.2001.1190;
RA   Peng X., Blum H., She Q., Mallok S., Bruegger K., Garrett R.A., Zillig W.,
RA   Prangishvili D.;
RT   "Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and
RT   SIRV2: relationships to the archaeal lipothrixvirus SIFV and some eukaryal
RT   viruses.";
RL   Virology 291:226-234(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate variant XX;
RX   PubMed=15469509; DOI=10.1111/j.1365-2958.2004.04287.x;
RA   Peng X., Kessler A., Phan H., Garrett R.A., Prangishvili D.;
RT   "Multiple variants of the archaeal DNA rudivirus SIRV1 in a single host and
RT   a novel mechanism of genomic variation.";
RL   Mol. Microbiol. 54:366-375(2004).
CC   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC       dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC       the intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. It does probably not deaminate dCTP.
CC       {ECO:0000269|PubMed:9497317}.
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:0000269|PubMed:9497317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9497317};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AF022221; AAC15873.1; -; Genomic_DNA.
DR   EMBL; AJ414696; CAC93972.1; -; Genomic_DNA.
DR   EMBL; AJ748296; CAG38836.1; -; Genomic_DNA.
DR   RefSeq; NP_666605.1; NC_004087.1.
DR   SMR; O71028; -.
DR   GeneID; 951366; -.
DR   KEGG; vg:951366; -.
DR   OrthoDB; 13481at10239; -.
DR   BRENDA; 3.6.1.23; 410.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000002270; Genome.
DR   Proteomes; UP000223181; Segment.
DR   GO; GO:0008829; F:dCTP deaminase activity; IEA:InterPro.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   HAMAP; MF_00146; dCTP_deaminase; 1.
DR   InterPro; IPR011962; dCTP_deaminase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   NCBIfam; TIGR02274; dCTP_deam; 1.
DR   PANTHER; PTHR42680; DCTP DEAMINASE; 1.
DR   PANTHER; PTHR42680:SF3; DCTP DEAMINASE; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..158
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000342288"
FT   VARIANT         10
FT                   /note="T -> R (in strain: Isolate variant XX)"
FT   VARIANT         15
FT                   /note="K -> N (in strain: Isolate variant XX)"
FT   VARIANT         20
FT                   /note="N -> D (in strain: Isolate variant XX)"
FT   VARIANT         133
FT                   /note="R -> H (in strain: Isolate variant XX)"
FT   VARIANT         148
FT                   /note="K -> N (in strain: Isolate variant XX)"
SQ   SEQUENCE   158 AA;  17906 MW;  5BA47765E0889190 CRC64;
     MILSDRDIKT YINSKKLVIN PLSEDTIREN GVDLKIGNEI VRIKENMEKE VGDEFIIYPN
     EHVLLTTKEY IKLSNDIIAF CNLRSTFARK GLLIPPTIVD AGFEGQLTIE LVGSSIPVKL
     KSGERFLHLI FARTLTPVEK PYNGKYQKQK GVTLAKED
//