uncharacterized protein [Chelonus insularis]
Protein Classification
site-specific integrase( domain architecture ID 10174512)
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 | |||||
| RNase_HI_RT_DIRS1 | cd09275 | DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ... |
86-205 | 1.33e-54 | |||||
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. : Pssm-ID: 260007 Cd Length: 120 Bit Score: 182.10 E-value: 1.33e-54
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| XerD super family | cl44177 | Site-specific recombinase XerD [Replication, recombination and repair]; |
349-619 | 5.30e-12 | |||||
Site-specific recombinase XerD [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG4974: Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 66.94 E-value: 5.30e-12
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| Name | Accession | Description | Interval | E-value | |||||
| RNase_HI_RT_DIRS1 | cd09275 | DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ... |
86-205 | 1.33e-54 | |||||
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. Pssm-ID: 260007 Cd Length: 120 Bit Score: 182.10 E-value: 1.33e-54
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| XerD | COG4974 | Site-specific recombinase XerD [Replication, recombination and repair]; |
349-619 | 5.30e-12 | |||||
Site-specific recombinase XerD [Replication, recombination and repair]; Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 66.94 E-value: 5.30e-12
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| RT_RNaseH_2 | pfam17919 | RNase H-like domain found in reverse transcriptase; |
57-144 | 2.06e-07 | |||||
RNase H-like domain found in reverse transcriptase; Pssm-ID: 465567 [Multi-domain] Cd Length: 100 Bit Score: 49.42 E-value: 2.06e-07
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| Phage_integrase | pfam00589 | Phage integrase family; Members of this family cleave DNA substrates by a series of staggered ... |
465-621 | 5.31e-05 | |||||
Phage integrase family; Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase are Arg-173, His-289, Arg-292 and Tyr-324. Pssm-ID: 395471 [Multi-domain] Cd Length: 169 Bit Score: 44.23 E-value: 5.31e-05
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| INT_Cre_C | cd00799 | C-terminal catalytic domain of Cre recombinase (also called integrase); Cre-like recombinases ... |
472-621 | 2.69e-04 | |||||
C-terminal catalytic domain of Cre recombinase (also called integrase); Cre-like recombinases 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 bacteriophage P1 Cre recombinase maintains the circular phage replicon in a monomeric state by catalyzing a site-specific recombination between two loxP sites. The catalytic core domain of Cre recombinase is linked to a more divergent helical N-terminal domain, which interacts primarily with the DNA major groove proximal to the crossover region. Pssm-ID: 271180 Cd Length: 188 Bit Score: 42.29 E-value: 2.69e-04
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| Name | Accession | Description | Interval | E-value | |||||
| RNase_HI_RT_DIRS1 | cd09275 | DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ... |
86-205 | 1.33e-54 | |||||
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. Pssm-ID: 260007 Cd Length: 120 Bit Score: 182.10 E-value: 1.33e-54
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| XerD | COG4974 | Site-specific recombinase XerD [Replication, recombination and repair]; |
349-619 | 5.30e-12 | |||||
Site-specific recombinase XerD [Replication, recombination and repair]; Pssm-ID: 443999 [Multi-domain] Cd Length: 291 Bit Score: 66.94 E-value: 5.30e-12
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| RT_RNaseH_2 | pfam17919 | RNase H-like domain found in reverse transcriptase; |
57-144 | 2.06e-07 | |||||
RNase H-like domain found in reverse transcriptase; Pssm-ID: 465567 [Multi-domain] Cd Length: 100 Bit Score: 49.42 E-value: 2.06e-07
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| RNase_HI_RT_Ty3 | cd09274 | Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ... |
86-203 | 2.56e-05 | |||||
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. Pssm-ID: 260006 [Multi-domain] Cd Length: 121 Bit Score: 44.02 E-value: 2.56e-05
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| Phage_integrase | pfam00589 | Phage integrase family; Members of this family cleave DNA substrates by a series of staggered ... |
465-621 | 5.31e-05 | |||||
Phage integrase family; Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase are Arg-173, His-289, Arg-292 and Tyr-324. Pssm-ID: 395471 [Multi-domain] Cd Length: 169 Bit Score: 44.23 E-value: 5.31e-05
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| RT_RNaseH | pfam17917 | RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ... |
86-178 | 1.97e-04 | |||||
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain. Pssm-ID: 465565 Cd Length: 104 Bit Score: 40.96 E-value: 1.97e-04
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| INT_Cre_C | cd00799 | C-terminal catalytic domain of Cre recombinase (also called integrase); Cre-like recombinases ... |
472-621 | 2.69e-04 | |||||
C-terminal catalytic domain of Cre recombinase (also called integrase); Cre-like recombinases 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 bacteriophage P1 Cre recombinase maintains the circular phage replicon in a monomeric state by catalyzing a site-specific recombination between two loxP sites. The catalytic core domain of Cre recombinase is linked to a more divergent helical N-terminal domain, which interacts primarily with the DNA major groove proximal to the crossover region. Pssm-ID: 271180 Cd Length: 188 Bit Score: 42.29 E-value: 2.69e-04
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| Blast search parameters | ||||
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