three-prime repair exonuclease 1 [Bos taurus]
Protein Classification
3'-5' exonuclease family protein; 3'-5' exonuclease( domain architecture ID 10150103)
3'-5' exonuclease family protein may cleave nucleotides one at a time from the end (exo) of a polynucleotide chain| 3'-5' exonuclease has a fundamental role in reducing polymerase errors and is involved in proofreading activity
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| TREX1_2 | cd06136 | DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar ... |
14-211 | 5.55e-73 | ||||
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins; Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture. : Pssm-ID: 99839 [Multi-domain] Cd Length: 177 Bit Score: 222.59 E-value: 5.55e-73
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| Name | Accession | Description | Interval | E-value | ||||
| TREX1_2 | cd06136 | DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar ... |
14-211 | 5.55e-73 | ||||
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins; Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture. Pssm-ID: 99839 [Multi-domain] Cd Length: 177 Bit Score: 222.59 E-value: 5.55e-73
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| DnaQ | COG0847 | DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
14-204 | 1.15e-08 | ||||
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair]; Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 53.64 E-value: 1.15e-08
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| EXOIII | smart00479 | exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
13-205 | 1.61e-08 | ||||
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases; Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 53.07 E-value: 1.61e-08
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| PRK09182 | PRK09182 | DNA polymerase III subunit epsilon; Validated |
7-123 | 7.04e-03 | ||||
DNA polymerase III subunit epsilon; Validated Pssm-ID: 236397 [Multi-domain] Cd Length: 294 Bit Score: 37.65 E-value: 7.04e-03
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| Name | Accession | Description | Interval | E-value | ||||
| TREX1_2 | cd06136 | DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar ... |
14-211 | 5.55e-73 | ||||
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins; Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture. Pssm-ID: 99839 [Multi-domain] Cd Length: 177 Bit Score: 222.59 E-value: 5.55e-73
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| DEDDh | cd06127 | DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
15-207 | 6.28e-12 | ||||
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others. Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 62.70 E-value: 6.28e-12
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| DnaQ | COG0847 | DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
14-204 | 1.15e-08 | ||||
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair]; Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 53.64 E-value: 1.15e-08
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| EXOIII | smart00479 | exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
13-205 | 1.61e-08 | ||||
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases; Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 53.07 E-value: 1.61e-08
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| PolC | COG2176 | DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
12-203 | 4.49e-05 | ||||
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 43.21 E-value: 4.49e-05
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| PRK09182 | PRK09182 | DNA polymerase III subunit epsilon; Validated |
7-123 | 7.04e-03 | ||||
DNA polymerase III subunit epsilon; Validated Pssm-ID: 236397 [Multi-domain] Cd Length: 294 Bit Score: 37.65 E-value: 7.04e-03
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| Blast search parameters | ||||
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