putative Integrase [Shigella flexneri]
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 | ||||
FimB super family | cl43194 | Integrase/recombinase, includes phage integrase [Replication, recombination and repair, ... |
9-209 | 6.16e-17 | ||||
Integrase/recombinase, includes phage integrase [Replication, recombination and repair, Mobilome: prophages, transposons]; The actual alignment was detected with superfamily member COG0582: Pssm-ID: 440347 [Multi-domain] Cd Length: 391 Bit Score: 78.16 E-value: 6.16e-17
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Name | Accession | Description | Interval | E-value | ||||
FimB | COG0582 | Integrase/recombinase, includes phage integrase [Replication, recombination and repair, ... |
9-209 | 6.16e-17 | ||||
Integrase/recombinase, includes phage integrase [Replication, recombination and repair, Mobilome: prophages, transposons]; Pssm-ID: 440347 [Multi-domain] Cd Length: 391 Bit Score: 78.16 E-value: 6.16e-17
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INT_P4_C | cd00801 | Bacteriophage P4 integrase, C-terminal catalytic domain; P4-like integrases are found in ... |
88-215 | 3.52e-16 | ||||
Bacteriophage P4 integrase, C-terminal catalytic domain; P4-like integrases are found in temperate bacteriophages, integrative plasmids, pathogenicity and symbiosis islands, and other mobile genetic elements. The P4 integrase mediates integrative and excisive site-specific recombination between two sites, called attachment sites, located on the phage genome and the bacterial chromosome. The phage attachment site is often found adjacent to the integrase gene, while the host attachment sites are typically situated near tRNA genes. This family belongs 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 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: 271182 [Multi-domain] Cd Length: 180 Bit Score: 73.07 E-value: 3.52e-16
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Name | Accession | Description | Interval | E-value | ||||
FimB | COG0582 | Integrase/recombinase, includes phage integrase [Replication, recombination and repair, ... |
9-209 | 6.16e-17 | ||||
Integrase/recombinase, includes phage integrase [Replication, recombination and repair, Mobilome: prophages, transposons]; Pssm-ID: 440347 [Multi-domain] Cd Length: 391 Bit Score: 78.16 E-value: 6.16e-17
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INT_P4_C | cd00801 | Bacteriophage P4 integrase, C-terminal catalytic domain; P4-like integrases are found in ... |
88-215 | 3.52e-16 | ||||
Bacteriophage P4 integrase, C-terminal catalytic domain; P4-like integrases are found in temperate bacteriophages, integrative plasmids, pathogenicity and symbiosis islands, and other mobile genetic elements. The P4 integrase mediates integrative and excisive site-specific recombination between two sites, called attachment sites, located on the phage genome and the bacterial chromosome. The phage attachment site is often found adjacent to the integrase gene, while the host attachment sites are typically situated near tRNA genes. This family belongs 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 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: 271182 [Multi-domain] Cd Length: 180 Bit Score: 73.07 E-value: 3.52e-16
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XerC | COG4973 | Site-specific recombinase XerC [Replication, recombination and repair]; |
2-209 | 2.27e-11 | ||||
Site-specific recombinase XerC [Replication, recombination and repair]; Pssm-ID: 443998 [Multi-domain] Cd Length: 287 Bit Score: 61.52 E-value: 2.27e-11
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XerD | COG4974 | Site-specific recombinase XerD [Replication, recombination and repair]; |
16-211 | 1.62e-10 | ||||
Site-specific recombinase XerD [Replication, recombination and repair]; Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 59.24 E-value: 1.62e-10
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INT_RitA_C_like | cd01188 | C-terminal catalytic domain of recombinase RitA, a component of the recombinase trio; ... |
90-203 | 1.77e-05 | ||||
C-terminal catalytic domain of recombinase RitA, a component of the recombinase trio; Recombinases RitA (also known as pAE1), RitB, and RitC are encoded by three adjacent and overlapping genes. Collectively they are known as the Recombinase in Trio (RIT). This RitA family includes various bacterial integrases and integrases from the deletion-prone region of plasmid pAE1 of Alcaligenes eutrophus H1. All three integrases contain a catalytic motif, suggesting that they are all active enzymes. However, their specific roles are not fully understood. All three families 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: 271188 [Multi-domain] Cd Length: 179 Bit Score: 43.77 E-value: 1.77e-05
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INTN1_C_like | cd01185 | Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal ... |
113-192 | 1.39e-04 | ||||
Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain; IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. This family belongs 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 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: 271185 [Multi-domain] Cd Length: 161 Bit Score: 40.71 E-value: 1.39e-04
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INT_Rci_Hp1_C | cd00796 | Shufflon-specific DNA recombinase Rci and Bacteriophage Hp1_like integrase, C-terminal ... |
82-209 | 3.59e-03 | ||||
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: 36.92 E-value: 3.59e-03
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Blast search parameters | ||||
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