HNH endonuclease [Bacillus cereus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Nuc_N | pfam14448 | Nuclease N terminal; This is a conserved short region that is found in many bacterial ... |
10-67 | 1.69e-26 | |||
Nuclease N terminal; This is a conserved short region that is found in many bacterial polymorphic toxin proteins. It is often located before C-terminal nuclease domains. : Pssm-ID: 373075 Cd Length: 58 Bit Score: 97.79 E-value: 1.69e-26
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HNHc super family | cl00083 | HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ... |
159-255 | 7.70e-21 | |||
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins. The actual alignment was detected with superfamily member pfam12639: Pssm-ID: 469607 Cd Length: 96 Bit Score: 84.44 E-value: 7.70e-21
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Name | Accession | Description | Interval | E-value | |||
Nuc_N | pfam14448 | Nuclease N terminal; This is a conserved short region that is found in many bacterial ... |
10-67 | 1.69e-26 | |||
Nuclease N terminal; This is a conserved short region that is found in many bacterial polymorphic toxin proteins. It is often located before C-terminal nuclease domains. Pssm-ID: 373075 Cd Length: 58 Bit Score: 97.79 E-value: 1.69e-26
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Colicin-DNase | pfam12639 | DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex ... |
159-255 | 7.70e-21 | |||
DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex structures with an N-terminal beta-barrel translocation domain (pfam09000), a long double-alpha-helical receptor-binding domain (pfam11570) and this C-terminal RNAse/DNase domain with endonuclease activity. Their competitor bacteriocidal action is by a process that involves binding to a surface receptor, entering the cell, and, finally, killing it. The lethal action of colicin E3 is a specific cleavage in the ribosomal decoding A site. The crystal structure of colicin E3 reveals a Y-shaped molecule with the receptor binding domain forming a 100 Angstrom long stalk and the two globular heads of the translocation domain and this catalytic domain comprising the two arms. Pssm-ID: 432688 Cd Length: 96 Bit Score: 84.44 E-value: 7.70e-21
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Name | Accession | Description | Interval | E-value | |||
Nuc_N | pfam14448 | Nuclease N terminal; This is a conserved short region that is found in many bacterial ... |
10-67 | 1.69e-26 | |||
Nuclease N terminal; This is a conserved short region that is found in many bacterial polymorphic toxin proteins. It is often located before C-terminal nuclease domains. Pssm-ID: 373075 Cd Length: 58 Bit Score: 97.79 E-value: 1.69e-26
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Colicin-DNase | pfam12639 | DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex ... |
159-255 | 7.70e-21 | |||
DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex structures with an N-terminal beta-barrel translocation domain (pfam09000), a long double-alpha-helical receptor-binding domain (pfam11570) and this C-terminal RNAse/DNase domain with endonuclease activity. Their competitor bacteriocidal action is by a process that involves binding to a surface receptor, entering the cell, and, finally, killing it. The lethal action of colicin E3 is a specific cleavage in the ribosomal decoding A site. The crystal structure of colicin E3 reveals a Y-shaped molecule with the receptor binding domain forming a 100 Angstrom long stalk and the two globular heads of the translocation domain and this catalytic domain comprising the two arms. Pssm-ID: 432688 Cd Length: 96 Bit Score: 84.44 E-value: 7.70e-21
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WHH | pfam14414 | A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of ... |
228-263 | 6.65e-09 | |||
A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif WHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. WHH is the shortest version of HNH nuclease families. Like AHH and LHH, the WHH nuclease contains 4 conserved histidines of which the first one is predicted to bind a metal-ion and other three ones are involved in activation of water molecule for hydrolysis. Pssm-ID: 433943 Cd Length: 43 Bit Score: 50.47 E-value: 6.65e-09
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Blast search parameters | ||||
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