A0A023W6Y9 · A0A023W6Y9_9CAUD

  • Protein
    Terminase, large subunit
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 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 packaged with the DNA, the terminase complex is substituted by the tail.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: ATPase activity requires 1 Mg2+ ion per subunit. Nuclease activity probably requires 2 Mg2+ ions per subunit.

Features

Showing features for binding site, active site, site.

161450100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site142ATP (UniProtKB | ChEBI)
Binding site147ATP (UniProtKB | ChEBI)
Binding site206ATP (UniProtKB | ChEBI)
Active site260For ATPase activity
Binding site404Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site404Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity
Site412Modulates nuclease activity
Binding site461Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site545Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity

GO annotations

AspectTerm
Cellular Componentviral terminase, large subunit
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Biological Processchromosome organization
Biological Processviral DNA genome packaging

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Terminase, large subunit
  • Alternative names
    • DNA-packaging protein

Including 2 domains:

  • Recommended name
    ATPase
  • EC number
  • Recommended name
    Endonuclease
  • EC number

Gene names

    • ORF names
      PS2_176

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Muldoonvirus > Muldoonvirus PS2

Accessions

  • Primary accession
    A0A023W6Y9

Proteomes

Subcellular Location

Interaction

Subunit

Interacts with the terminase small subunit; the active complex is probably heterooligomeric. Interacts with the portal protein.

Family & Domains

Features

Showing features for motif, domain.

Type
IDPosition(s)Description
Motif165-171Walker A motif
Motif255-260Walker B motif
Motif289-291ATPase coupling
Domain402-574Terminase large subunit gp17-like C-terminal

Domain

The N-terminus contains an ATPase domain. The C-terminus contains an endonuclease domain.

Sequence similarities

Belongs to the Tequatrovirus large terminase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    69,807
  • Last updated
    2014-07-09 v1
  • MD5 Checksum
    EDD989F998C064F5502A0AF1DFA5EE6A
MSEDTLQSTENLNVLADDAHPLGDWIKAPSALETKIEDGVKFFRSQWDDKWYPEKFSDYLRLHGIVKVALQGEDPSKFQTFKDKNNKRTRYLGLPNLKRANIKTAWTAEMVKEWKKCRDDIVYFAETYCAITHIDYGVIKVQLRDYQRDMLKIMARDRMVTCNLSRQLGKTTVVAIFLAHFVCFNRAKAVGILAHKGSMSAEVLDRTKQAIELLPDFLQPGIVEWNKGSIELDNGSSIGAYASSPDAVRGNSFALIYIDECAFIPNFHDAWLAIQPVISSGRRSKIIITTTPNGLNHFYDIWTAAVEGTSGFTPYNAIWNSVKERLYDKDDMFDDGWQWSAQTIFASSLEQFKQEHCAEFHGTSGTLISGLKLGGMTWTEIVPEQGFYRFKDPEEGHKYIATLDSAEGRGQDYHAMHIIDVTNFPFEQVAVFHNNTTSHLILPDVLMRYLNEYNEAAIYVELNSTGVSVAKSLYMDLEYENVICDSYQDLGMKQTKRTKAVGCSTLKDLIEKDKLIIHHRPTIAEFRTFSEKGVSWAAEDGYHDDLVMGLVIFAWLSTQQKFADFLGKDELRIANEVFRKELEDMDDDYAPVIIVDNAQGAYEVEPSSHGLSFV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ025957
EMBL· GenBank· DDBJ
AHY25517.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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