ID A0A0M4NHP0_9ADEN Unreviewed; 126 AA.
AC A0A0M4NHP0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
OS Simian adenovirus 19.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Simian mastadenovirus C.
OX NCBI_TaxID=38416 {ECO:0000313|EMBL:ALE30454.1, ECO:0000313|Proteomes:UP000129765};
RN [1] {ECO:0000313|EMBL:ALE30454.1, ECO:0000313|Proteomes:UP000129765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AA153 {ECO:0000313|EMBL:ALE30454.1};
RX PubMed=26370792; DOI=10.1007/s00705-015-2575-z;
RA Panto L., Podgorski I.I., Janoska M., Marko O., Harrach B.;
RT "Taxonomy proposal for Old World monkey adenoviruses: characterisation of
RT several non-human, non-ape primate adenovirus lineages.";
RL Arch. Virol. 160:3165-3177(2015).
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. {ECO:0000256|ARBA:ARBA00003495}.
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KP329565; ALE30454.1; -; Genomic_DNA.
DR RefSeq; YP_009174217.1; NC_028107.1.
DR GeneID; 26100739; -.
DR KEGG; vg:26100739; -.
DR OrthoDB; 16798at10239; -.
DR Proteomes; UP000129765; Genome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
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 Reference proteome {ECO:0000313|Proteomes:UP000129765}.
FT DOMAIN 16..118
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 126 AA; 14298 MW; ADA0E60C582FB4E6 CRC64;
MADEAIYVHL LGSWAIMPQQ QGFSNLYVLF SPENFVIPPR GVLLVSLQLS MDIPQGYLGR
LFSLSDMNVR GVFVGAQDIQ PSTWWEMSVV LFNHSDEFFY GFRGQPVACL LLERVIYPCL
HRASLV
//
