hypothetical protein Q182_02448, partial [Staphylococcus aureus M1180]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| trimeric_dUTPase super family | cl00493 | Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ... |
1-24 | 1.57e-05 | ||
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface. The actual alignment was detected with superfamily member PRK00601: Pssm-ID: 444938 [Multi-domain] Cd Length: 150 Bit Score: 37.45 E-value: 1.57e-05
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| Name | Accession | Description | Interval | E-value | ||
| dut | PRK00601 | dUTP diphosphatase; |
1-24 | 1.57e-05 | ||
dUTP diphosphatase; Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 37.45 E-value: 1.57e-05
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| Dut | COG0756 | dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
1-24 | 5.76e-05 | ||
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 35.76 E-value: 5.76e-05
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| dut | TIGR00576 | deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
1-24 | 9.83e-03 | ||
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); 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. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism] Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 29.89 E-value: 9.83e-03
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| Name | Accession | Description | Interval | E-value | ||
| dut | PRK00601 | dUTP diphosphatase; |
1-24 | 1.57e-05 | ||
dUTP diphosphatase; Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 37.45 E-value: 1.57e-05
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| Dut | COG0756 | dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
1-24 | 5.76e-05 | ||
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 35.76 E-value: 5.76e-05
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| dut | TIGR00576 | deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
1-24 | 9.83e-03 | ||
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); 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. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism] Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 29.89 E-value: 9.83e-03
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