DNA polymerase beta, partial [Xiphophorus continens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DNA_pol_B_palm | pfam14792 | DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ... |
15-95 | 3.36e-38 | |||
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain. : Pssm-ID: 464318 Cd Length: 110 Bit Score: 123.44 E-value: 3.36e-38
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Name | Accession | Description | Interval | E-value | |||
DNA_pol_B_palm | pfam14792 | DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ... |
15-95 | 3.36e-38 | |||
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain. Pssm-ID: 464318 Cd Length: 110 Bit Score: 123.44 E-value: 3.36e-38
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NT_POLXc | cd00141 | Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ... |
1-96 | 2.36e-34 | |||
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family. Pssm-ID: 143386 [Multi-domain] Cd Length: 307 Bit Score: 119.22 E-value: 2.36e-34
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POLXc | smart00483 | DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
1-96 | 2.07e-25 | |||
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases Pssm-ID: 214688 Cd Length: 334 Bit Score: 96.28 E-value: 2.07e-25
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PolX | COG1796 | DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
2-96 | 4.11e-09 | |||
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 51.73 E-value: 4.11e-09
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Name | Accession | Description | Interval | E-value | |||
DNA_pol_B_palm | pfam14792 | DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ... |
15-95 | 3.36e-38 | |||
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain. Pssm-ID: 464318 Cd Length: 110 Bit Score: 123.44 E-value: 3.36e-38
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NT_POLXc | cd00141 | Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ... |
1-96 | 2.36e-34 | |||
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family. Pssm-ID: 143386 [Multi-domain] Cd Length: 307 Bit Score: 119.22 E-value: 2.36e-34
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POLXc | smart00483 | DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
1-96 | 2.07e-25 | |||
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases Pssm-ID: 214688 Cd Length: 334 Bit Score: 96.28 E-value: 2.07e-25
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PolX | COG1796 | DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
2-96 | 4.11e-09 | |||
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 51.73 E-value: 4.11e-09
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NT_Pol-beta-like | cd05397 | Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ... |
22-62 | 1.75e-04 | |||
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes. Pssm-ID: 143387 [Multi-domain] Cd Length: 49 Bit Score: 36.15 E-value: 1.75e-04
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Blast search parameters | ||||
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