ID Q9B001_9CAUD Unreviewed; 139 AA.
AC Q9B001;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN Name=orf28 {ECO:0000313|EMBL:AAK08253.1};
OS Lactococcus phage bIL285.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=151535 {ECO:0000313|EMBL:AAK08253.1, ECO:0000313|Proteomes:UP000002583};
RN [1] {ECO:0000313|EMBL:AAK08253.1, ECO:0000313|Proteomes:UP000002583}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11160885; DOI=10.1093/nar/29.3.644;
RA Chopin A., Bolotin A., Sorokin A., Ehrlich S.D., Chopin M.;
RT "Analysis of six prophages in Lactococcus lactis IL1403: different genetic
RT structure of temperate and virulent phage populations.";
RL Nucleic Acids Res. 29:644-651(2001).
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; AF323668; AAK08253.1; -; Genomic_DNA.
DR RefSeq; NP_076600.1; NC_002666.1.
DR GeneID; 920252; -.
DR KEGG; vg:920252; -.
DR OrthoDB; 12539at10239; -.
DR Proteomes; UP000002583; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002583}.
FT DOMAIN 11..137
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 139 AA; 15196 MW; 45AEB1D92FF390BC CRC64;
MTRGFKKLDE NATIPERATE HSAGYDISAS ETVTIQPDEI KMVSTGLAVQ LGDDEVLKLY
DRSSNPVKRG IALINSVGII DSDYYPQEFK GLFMNISKEP VTISKGQRIM QGVFVKYLTT
NDDNANGKRT GGFGSTGEV
//
