A0A5Q2F3P4 · A0A5Q2F3P4_9CAUD
- ProteinTerminase, large subunit
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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 at a unique and precise dsDNA sequence 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 DNA is packaged, the terminase detaches from the portal and gets replaced by the tail to finish maturation of the virion.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 365 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity | ||||
Sequence: D | ||||||
Binding site | 365 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity | ||||
Sequence: D | ||||||
Binding site | 420 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity | ||||
Sequence: E | ||||||
Binding site | 518 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | viral terminase, large subunit | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | endonuclease activity | |
Molecular Function | metal ion binding | |
Biological Process | chromosome organization | |
Biological Process | viral DNA genome packaging |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTerminase, large subunit
- Alternative names
Including 2 domains:
- Recommended nameATPase
- EC number
- Recommended nameEndonuclease
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Autographiviridae > Studiervirinae > Przondovirus > Przondovirus Kp1
Accessions
- Primary accessionA0A5Q2F3P4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homopentamer. Interacts with the terminase small subunit; the active complex is probably heterooligomeric. Interacts with the portal protein.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 59-66 | Walker A motif | ||||
Sequence: AFRGIGKS | ||||||
Motif | 157-162 | Walker B motif | ||||
Sequence: IIIADD |
Domain
The ATPase region is in the N-terminus, whereas the nuclease region is in the central part. The C-terminus is involved in prohead binding.
Sequence similarities
Belongs to the Teseptimavirus large terminase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length585
- Mass (Da)66,184
- Last updated2020-02-26 v1
- Checksum491B3115CEB180B2