HAMAP rule MF_04145
General rule information
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Accession | MF_04145 |
Dates | 17-JAN-2020 (Created)
1-JUN-2023 (Last updated, Version 9) |
Name | TERL_SPP1 |
Scope(s) |
Viruses Caudoviricetes |
Template(s) | P54308 (TERL_BPSPP); [ Recover all ] |
Triggered by |
HAMAP; MF_04145 (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; Includes: RecName: Full=Endonuclease; EC=3.1.-.-; Includes: RecName: Full=ATPase; EC=3.6.4.-; |
Comments
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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 adapter and the stopper protein that form the connector. |
case <FTGroup:1> | |
COFACTOR | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 divalent metal cations per subunit. Mn(2+) is preferred over Mg(2+).; |
end case | |
SUBUNIT | Monomer. Interacts with the terminase small subunit; the active complex is probably heterooligomeric. Interacts with the portal protein. |
DOMAIN | The N-terminus contains an ATPase domain and the C-terminus contains an endonuclease domain. |
Keywords
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ATP-binding | |
Endonuclease | |
Nucleotide-binding | |
Hydrolase | |
case <FTGroup:1> | |
Magnesium | |
Manganese | |
Metal-binding | |
end case | |
Nuclease | |
Viral genome packaging | |
Viral release from host cell |
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_BPSPP (P54308) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REGION | 1 | 198 | /note="ATPase activity" | |||||||||
REGION | 232 | 422 | /note="Nuclease activity and binding to the portal protein" | |||||||||
MOTIF | 33 | 40 | /note="Walker A motif" | G-[GS]-[AR]-[AG]-S-[AGK]-[AGK]-S | ||||||||
MOTIF | 130 | 135 | /note="Walker B motif" | x-[CAGLM]-W-[IFY]-E-E | ||||||||
ACT_SITE | 135 | 135 | /note="For ATPase activity" | E | ||||||||
BINDING | 266 | 266 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" /ligand_note="catalytic; for nuclease activity" |
D | 1 | |||||||
BINDING | 266 | 266 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" /ligand_note="catalytic; for nuclease activity" |
D | 1 | |||||||
BINDING | 321 | 321 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" /ligand_note="catalytic; for nuclease activity" |
D | 1 | |||||||
BINDING | 400 | 400 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" /ligand_note="catalytic; for nuclease activity" |
H | 1 | |||||||
BINDING | 403 | 403 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" /ligand_note="catalytic; for nuclease activity" |
D | 1 |
Additional information
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Size range | 370-540 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |