integrase [Bacillus toyonensis]
site-specific integrase( domain architecture ID 332)
tyrosine based site-specific recombinase (integrase) is involved in cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
DNA_BRE_C super family | cl00213 | DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme ... |
392-564 | 6.37e-06 | ||||
DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity. The actual alignment was detected with superfamily member cd00397: Pssm-ID: 469662 [Multi-domain] Cd Length: 167 Bit Score: 47.09 E-value: 6.37e-06
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Name | Accession | Description | Interval | E-value | ||||
DNA_BRE_C | cd00397 | DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme ... |
392-564 | 6.37e-06 | ||||
DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity. Pssm-ID: 271175 [Multi-domain] Cd Length: 167 Bit Score: 47.09 E-value: 6.37e-06
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XerD | COG4974 | Site-specific recombinase XerD [Replication, recombination and repair]; |
401-581 | 1.18e-05 | ||||
Site-specific recombinase XerD [Replication, recombination and repair]; Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 47.68 E-value: 1.18e-05
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Name | Accession | Description | Interval | E-value | ||||
DNA_BRE_C | cd00397 | DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme ... |
392-564 | 6.37e-06 | ||||
DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity. Pssm-ID: 271175 [Multi-domain] Cd Length: 167 Bit Score: 47.09 E-value: 6.37e-06
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XerD | COG4974 | Site-specific recombinase XerD [Replication, recombination and repair]; |
401-581 | 1.18e-05 | ||||
Site-specific recombinase XerD [Replication, recombination and repair]; Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 47.68 E-value: 1.18e-05
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INT_Rci_Hp1_C | cd00796 | Shufflon-specific DNA recombinase Rci and Bacteriophage Hp1_like integrase, C-terminal ... |
400-564 | 1.25e-05 | ||||
Shufflon-specific DNA recombinase Rci and Bacteriophage Hp1_like integrase, C-terminal catalytic domain; Rci protein is a tyrosine recombinase specifically involved in Shufflon type of DNA rearrangement in bacteria. The shufflon of plasmid R64 consists of four invertible DNA segments which are separated and flanked by seven 19-bp repeat sequences. RCI recombinase facilitates the site-specific recombination between any inverted repeats results in an inversion of the DNA segment(s) either independently or in groups. HP1 integrase promotes site-specific recombination of the HP1 genome into that of Haemophilus influenza. Bacteriophage Hp1_like integrases are tyrosine based site specific recombinases. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Pssm-ID: 271177 [Multi-domain] Cd Length: 162 Bit Score: 46.17 E-value: 1.25e-05
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XerC | COG4973 | Site-specific recombinase XerC [Replication, recombination and repair]; |
393-576 | 5.42e-04 | ||||
Site-specific recombinase XerC [Replication, recombination and repair]; Pssm-ID: 443998 [Multi-domain] Cd Length: 287 Bit Score: 42.64 E-value: 5.42e-04
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Blast search parameters | ||||
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