Summary
dUTPase
dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
Literature references
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Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS; , Nature 1992;355:740-743.: Crystal structure of a dUTPase. PUBMED:1311056
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Mol CD, Harris JM, McIntosh EM, Tainer JA; , Structure 1996;4:1077-1092.: Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. PUBMED:8805593
InterPro entry IPR008180
Synonym(s): dUTP diphosphatase, Deoxyuridine-triphosphatase
The essential enzyme dUTP pyrophosphatase () is specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. dUTPase decreases the intracellular concentration of dUPT so that uracil cannot be incorporated into DNA PUBMED:8805593.
The crystal structure of human dUTPase reveals that each subunit of the dUTPase trimer folds into an eight-stranded jelly-roll beta barrel, with the C-terminal beta strands interchanged among the subunits. The structure is similar to that of the Escherichia coli enzyme, despite low sequence homology between the two enzymes PUBMED:8805593.
Other enzymes like deoxycytidine triphosphate deaminase (dCTP) () that specifically bind uridine also belong to this group suggesting that the signature may recognise a putative uridine-binding motif.
Some retroviruses encode dUTPases. Retroviral dUTPase is synthesised as part of POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, dUTPase and RNase H.
Clan
This family is a member of clan dUTPase (CL0153), which contains the following 7 members:
Cytomega_UL84 DCD DUF570 dUTPase Herpes_ORF11 Herpes_U55 Herpes_UL82_83Gene Ontology
| Molecular function | hydrolase activity (GO:0016787) |
| Biological process | dUTP metabolic process (GO:0046080) |
External database links
| HOMSTRAD: | dutpase |
| PANDIT: | PF00692 |
| SCOP: | 1dup |
| SYSTERS: | dUTPase |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_127 (release 2.1) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 29 |
| Number in full: | 2899 |
| Average length of the domain: | 122.10 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 58.51 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 129 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
dUTPaseStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the dUTPase domain has been found.
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