DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit ...
111-238
1.37e-07
DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit B N-terminal domain which is involved in complex formation. This domain adopts an OB fold.
The actual alignment was detected with superfamily member pfam08418:
Pssm-ID: 462470 Cd Length: 240 Bit Score: 52.72 E-value: 1.37e-07
DNA polymerase alpha/epsilon subunit B; This family contains a number of DNA polymerase ...
342-549
1.07e-66
DNA polymerase alpha/epsilon subunit B; This family contains a number of DNA polymerase subunits. The B subunit of the DNA polymerase alpha plays an essential role at the initial stage of DNA replication in S. cerevisiae and is phosphorylated in a cell cycle-dependent manner. DNA polymerase epsilon is essential for cell viability and chromosomal DNA replication in budding yeast. In addition, DNA polymerase epsilon may be involved in DNA repair and cell-cycle checkpoint control. The enzyme consists of at least four subunits in mammalian cells as well as in yeast. The largest subunit of DNA polymerase epsilon is responsible for polymerase epsilon is responsible for polymerase activity. In mouse, the DNA polymerase epsilon subunit B is the second largest subunit of the DNA polymerase. A part of the N-terminal was found to be responsible for the interaction with SAP18. Experimental evidence suggests that this subunit may recruit histone deacetylase to the replication fork to modify the chromatin structure.
Pssm-ID: 461142 Cd Length: 210 Bit Score: 216.41 E-value: 1.07e-66
DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit ...
111-238
1.37e-07
DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit B N-terminal domain which is involved in complex formation. This domain adopts an OB fold.
Pssm-ID: 462470 Cd Length: 240 Bit Score: 52.72 E-value: 1.37e-07
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small ...
407-560
1.84e-05
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small subunit of the archeal DNA polymerase II contains a C-terminal metallophosphatase domain. This domain is thought to be functionally active because the active site residues required for phosphoesterase activity in other members of this superfamily are intact. The archeal replicative DNA polymerases are thought to possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277332 Cd Length: 243 Bit Score: 46.53 E-value: 1.84e-05
DNA polymerase alpha/epsilon subunit B; This family contains a number of DNA polymerase ...
342-549
1.07e-66
DNA polymerase alpha/epsilon subunit B; This family contains a number of DNA polymerase subunits. The B subunit of the DNA polymerase alpha plays an essential role at the initial stage of DNA replication in S. cerevisiae and is phosphorylated in a cell cycle-dependent manner. DNA polymerase epsilon is essential for cell viability and chromosomal DNA replication in budding yeast. In addition, DNA polymerase epsilon may be involved in DNA repair and cell-cycle checkpoint control. The enzyme consists of at least four subunits in mammalian cells as well as in yeast. The largest subunit of DNA polymerase epsilon is responsible for polymerase epsilon is responsible for polymerase activity. In mouse, the DNA polymerase epsilon subunit B is the second largest subunit of the DNA polymerase. A part of the N-terminal was found to be responsible for the interaction with SAP18. Experimental evidence suggests that this subunit may recruit histone deacetylase to the replication fork to modify the chromatin structure.
Pssm-ID: 461142 Cd Length: 210 Bit Score: 216.41 E-value: 1.07e-66
DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit ...
111-238
1.37e-07
DNA polymerase alpha subunit B N-terminal; This is the eukaryotic DNA polymerase alpha subunit B N-terminal domain which is involved in complex formation. This domain adopts an OB fold.
Pssm-ID: 462470 Cd Length: 240 Bit Score: 52.72 E-value: 1.37e-07
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small ...
407-560
1.84e-05
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small subunit of the archeal DNA polymerase II contains a C-terminal metallophosphatase domain. This domain is thought to be functionally active because the active site residues required for phosphoesterase activity in other members of this superfamily are intact. The archeal replicative DNA polymerases are thought to possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277332 Cd Length: 243 Bit Score: 46.53 E-value: 1.84e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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