DUT_HHV6U
ID DUT_HHV6U Reviewed; 376 AA.
AC Q06095;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 02-JUN-2021, entry version 83.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031};
GN Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; OrderedLocusNames=U45;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1333836; DOI=10.3109/10425179209039693;
RA Gompels U.A., Carss A.L., Sun N., Arrand J.R.;
RT "Infectivity determinants encoded in a conserved gene block of human
RT herpesvirus-6.";
RL DNA Seq. 3:25-39(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
CC -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the
CC immediate precursor of thymidine nucleotides and decreases the
CC intracellular concentration of dUTP to avoid uracil incorporation into
CC viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}.
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:0000255|HAMAP-Rule:MF_04031};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_04031}.
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DR EMBL; X64320; CAA45600.1; -; Genomic_DNA.
DR EMBL; X83413; CAA58379.1; -; Genomic_DNA.
DR EMBL; X92436; CAA63171.1; -; Genomic_DNA.
DR PIR; A56653; A56653.
DR RefSeq; NP_042938.1; NC_001664.2.
DR SMR; Q06095; -.
DR PRIDE; Q06095; -.
DR DNASU; 1487924; -.
DR GeneID; 1487924; -.
DR KEGG; vg:1487924; -.
DR Proteomes; UP000009295; Genome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.70.40.10; -; 2.
DR HAMAP; MF_04031; HSV_DUT; 1.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR034745; HSV_DUT.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 2.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182959"
SQ SEQUENCE 376 AA; 43398 MW; 81B3CE9C817D27D5 CRC64;
MYSAISEKIS ETITLQRQTS SRYIEFFVFR NVDINELWTT DISEDKTHDV WPAVNEKSFK
KFLENELTSY QRPIPLLGIP QNGTVSKTCK KEKQRETDCV NYERKRGNPV TFYPRHRAKR
NANTDTCISE EPSILVSHHR NSKMDVFMDT NKITLVNREL IWVPHDQVRI VKLDISLYIP
DGFFGVITGH SNDVFCECVT EIITDETDIS VFLMNLSEHS LMLLPGDVEF SINFLPCYIP
EPWEMINLSP PEFAIFHLKA SREFIAKPNS YTIQYFDAMY VCADELKALM IPSKEIAKLG
LLIETYIWNK DTIPSIKIFN STRKTIYIPT GICIARIIFT CGHFCLSLMP ERAINRLQVL
DANSSFLFHY AASNNA