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(s) |
Viruses |
| Template(s) | P26745 (TERL_BPP22); [ Recover all ] |
| Triggered by |
HAMAP; MF_04148 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | TERL |
| Protein name | RecName: Full=Terminase, large subunit; AltName: Full=DNA-packaging protein gp2; Includes: RecName: Full=Endonuclease; EC=3.1.21.-; Includes: RecName: Full=ATPase; EC=3.6.4.-; |
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 | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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 | |
| case <FTGroup:1> | |
| Magnesium | |
| Metal-binding | |
| 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 |
Cross-references
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Features
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| From: TERL_BPP22 (P26745) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Lederbergvirus> | ||||||||||||
| REGION | 1 | 58 | /note="Interaction with the terminase small subunit" | |||||||||
| REGION | 1 | 286 | /note="ATPase activity" | |||||||||
| REGION | 312 | 482 | /note="Nuclease activity" | |||||||||
| end case | ||||||||||||
| MOTIF | 60 | 67 | /note="Walker A motif" | [ACT]-[AG]-N-[QR]-[CILV]-G-K-[ST] | ||||||||
| MOTIF | 199 | 204 | /note="Walker B motif" | [FGILVWY]-[FIV]-[WH]-[FILM]-D-E | ||||||||
| ACT_SITE | 204 | 204 | /note="For ATPase activity" | E | ||||||||
| BINDING | 321 | 321 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic; for nuclease activity" |
D | 1 | |||||||
| BINDING | 459 | 459 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic; for nuclease activity" |
D | 1 | |||||||
Additional information
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| Size range | 400-530 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |