ID A5GYU3_9CAUD Unreviewed; 139 AA.
AC A5GYU3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
OS Lactococcus phage ul36.t1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=374527 {ECO:0000313|EMBL:ABD63771.1, ECO:0000313|Proteomes:UP000001579};
RN [1] {ECO:0000313|EMBL:ABD63771.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17041060; DOI=10.1128/JB.01111-06;
RA Labrie S.J., Moineau S.;
RT "Abortive infection mechanisms and prophage sequences significantly
RT influence the genetic makeup of emerging lytic lactococcal phages.";
RL J. Bacteriol. 189:1482-1487(2007).
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
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DR EMBL; DQ394808; ABD63771.1; -; Genomic_DNA.
DR Proteomes; UP000001579; Genome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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 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}.
FT DOMAIN 12..137
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 139 AA; 15307 MW; AE5FFEB1E71EEE79 CRC64;
MKRKFLKLNT QAIKPERATK HSAGYDISSS ETVTIQPDEI KMVSTGLAVQ LGDDEVLKLY
DRSSNPVKRG IALINSVGII DSDYYPQEFK GLFMNISKEP VTISKGQRIM QGVFVKYLTT
DDDNANGKRT GGFGSTGEV
//
