U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 7

1.

dCTP deaminase domain-containing protein

This entry represents a dCTP deaminase (DCD) domain found in archaea and bacteria [1-5]. Methanococcus jannaschii, has a bifunctional enzyme DCD-DUT, that harbors both dCTP deaminase and dUTP pyrophosphatase activities [1]. Paper describing PDB structure 1ogh. [1]. 12756253. Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases. Johansson E, Bjornberg O, Nyman PO, Larsen S;. J Biol Chem. 2003;278:27916-27922. Paper describing PDB structure 1xs1. [2]. 15539408. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. Johansson E, Fano M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoes M;. J Biol Chem. 2005;280:3051-3059. Paper describing PDB structure 2j4h. [3]. 17651436. Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme. Johansson E, Thymark M, Bynck JH, Fano M, Larsen S, Willemoes M;. FEBS J. 2007;274:4188-4198. Paper describing PDB structure 2qlp. [4]. 18164314. Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis. Helt SS, Thymark M, Harris P, Aagaard C, Dietrich J, Larsen S, Willemoes M;. J Mol Biol. 2008;376:554-569. Paper describing PDB structure 2v9x. [5]. 17996716. Mutational analysis of the nucleotide binding site of Escherichia coli dCTP deaminase. Thymark M, Johansson E, Larsen S, Willemoes M;. Arch Biochem Biophys. 2008;470:20-26. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046371.1
Method:
HMM
2.

dUTPase

dUTPase hydrolyses dUTP to dUMP and pyrophosphate. [1]. 1311056. Crystal structure of a dUTPase. Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS;. Nature 1992;355:740-743. [2]. 8805593. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Mol CD, Harris JM, McIntosh EM, Tainer JA;. Structure 1996;4:1077-1092. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012895.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

dUTP diphosphatase

dUTP diphosphatase is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA

Date:
2023-03-07
Family Accession:
10792031
Method:
Sparcle
6.

dUTP diphosphatase

Gene:
dut
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
dUTP diphosphatase activity (GO:0004170)
Biological Process:
dUMP biosynthetic process (GO:0006226)
Biological Process:
dUTP catabolic process (GO:0046081)
Date:
2021-07-22
Family Accession:
NF001862.0
Method:
HMM
7.

dUTP diphosphatase

The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. The enzyme occurs in bacteria, viruses including prophage regions, and eukaryotes.

Gene:
dut
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
dUTP diphosphatase activity (GO:0004170)
Biological Process:
dUMP biosynthetic process (GO:0006226)
Biological Process:
dUTP catabolic process (GO:0046081)
Date:
2024-05-16
Family Accession:
TIGR00576.1
Method:
HMM
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center