HAMAP rule MF_04148
General rule information
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Accession | MF_04148 |
Dates | 18-FEB-2020 (Created) 19-NOV-2022 (Last updated, Version 5) |
Name | TERL_BPP22 |
Scope | Viruses |
Template | P26745 (TERL_BPP22) |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Comments
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case <OC:Lederbergvirus>
Function | The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. |
else
Function | The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Once the capsid is packaged with the DNA, the terminase cleaves the viral genome concatemer and is substituted by the tail. |
end case
case <FTGroup:1>
Cofactor | Mg(2+) Note: Nuclease activity probably requires 2 Mg(2+) ions per subunit |
end case
Subunit | Interacts with the terminase small subunit; the active complex is composed of a monomer of the terminase large subunit and a nonamer ring of terminase small subunits. Interacts with the portal protein; this interaction allows the packaging of viral DNA. |
Domain | The ATPase region is in the N-terminus, whereas the nuclease region is in the C-terminus. |
Similarity | Belongs to the Lederbergvirus large terminase family. |
Keywords
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ATP-binding
Endonuclease
Hydrolase
Late protein
Nuclease
Nucleotide-binding
Viral genome packaging
Viral release from host cell
Endonuclease
Hydrolase
Late protein
Nuclease
Nucleotide-binding
Viral genome packaging
Viral release from host cell
case <FTGroup:1>
end case
Gene Ontology
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GO:0098009; Cellular component: viral terminase, large subunit.
GO:0004519; Molecular function: endonuclease activity.
GO:0046872; Molecular function: metal ion binding.
GO:0004518; Molecular function: nuclease activity.
GO:0051276; Biological process: chromosome organization.
GO:0019073; Biological process: viral DNA genome packaging.
GO:0004519; Molecular function: endonuclease activity.
GO:0046872; Molecular function: metal ion binding.
GO:0004518; Molecular function: nuclease activity.
GO:0051276; Biological process: chromosome organization.
GO:0019073; Biological process: viral DNA genome packaging.
Cross-references
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Features
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case <OC:Lederbergvirus>
From: TERL_BPP22 (P26745) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REGION | 1 | 58 | Interaction with the terminase small subunit | |||||||||
REGION | 1 | 286 | ATPase activity | |||||||||
REGION | 312 | 482 | Nuclease activity |
end case
Additional information
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Size range | 400-530 amino acids |
Related rules | None |
Fusion | None |