P03694 · TERL_BPT7
- ProteinTerminase, large subunit
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids586 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 (By similarity).
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 (By similarity).
Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine (PubMed:23632014).
The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer (By similarity).
Once the DNA is packaged, the terminase detaches from the portal and gets replaced by the tail to finish maturation of the virion (PubMed:23632014).
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 (By similarity).
Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine (PubMed:23632014).
The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer (By similarity).
Once the DNA is packaged, the terminase detaches from the portal and gets replaced by the tail to finish maturation of the virion (PubMed:23632014).
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 364 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity | ||||
Sequence: D | ||||||
Binding site | 364 | 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
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Autographiviridae > Studiervirinae > Teseptimavirus > Teseptimavirus T7
- Virus hosts
Accessions
- Primary accessionP03694
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000106541 | 1-586 | Terminase, large subunit | |||
Sequence: MSTQSNRNALVVAQLKGDFVAFLFVLWKALNLPVPTKCQIDMAKVLANGDNKKFILQAFRGIGKSFITCAFVVWSLWRDPQLKILIVSASKERADANSIFIKNIIDLLPFLSELKPRPGQRDSVISFDVGPANPDHSPSVKSVGITGQLTGSRADIIIADDVEIPSNSATMGAREKLWTLVQEFAALLKPLPSSRVIYLGTPQTEMTLYKELEDNRGYTTIIWPALYPRTREENLYYSQRLAPMLRAEYDENPEALAGTPTDPVRFDRDDLRERELEYGKAGFTLQFMLNPNLSDAEKYPLRLRDAIVAALDLEKAPMHYQWLPNRQNIIEDLPNVGLKGDDLHTYHDCSNNSGQYQQKILVIDPSGRGKDETGYAVLYTLNGYIYLMEAGGFRDGYSDKTLELLAKKAKQWGVQTVVYESNFGDGMFGKVFSPILLKHHNCAMEEIRARGMKEMRICDTLEPVMQTHRLVIRDEVIRADYQSARDVDGKHDVKYSLFYQMTRITREKGALAHDDRLDALALGIEYLRESMQLDSVKVEGEVLADFLEEHMMRPTVAATHIIEMSVGGVDVYSEDDEGYGTSFIEW |
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-229 | ATPase activity | ||||
Sequence: MSTQSNRNALVVAQLKGDFVAFLFVLWKALNLPVPTKCQIDMAKVLANGDNKKFILQAFRGIGKSFITCAFVVWSLWRDPQLKILIVSASKERADANSIFIKNIIDLLPFLSELKPRPGQRDSVISFDVGPANPDHSPSVKSVGITGQLTGSRADIIIADDVEIPSNSATMGAREKLWTLVQEFAALLKPLPSSRVIYLGTPQTEMTLYKELEDNRGYTTIIWPALYPR | ||||||
Motif | 58-65 | Walker A motif | ||||
Sequence: AFRGIGKS | ||||||
Motif | 156-161 | Walker B motif | ||||
Sequence: IIIADD | ||||||
Region | 344-429 | Nuclease activity | ||||
Sequence: HTYHDCSNNSGQYQQKILVIDPSGRGKDETGYAVLYTLNGYIYLMEAGGFRDGYSDKTLELLAKKAKQWGVQTVVYESNFGDGMFG | ||||||
Region | 571-586 | Involved in prohead binding | ||||
Sequence: VYSEDDEGYGTSFIEW |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length586
- Mass (Da)66,261
- Last updated1986-07-21 v1
- Checksum0030B8EE701CB0A9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V01146 EMBL· GenBank· DDBJ | CAA24440.1 EMBL· GenBank· DDBJ | Genomic DNA |