A0A060QNT8 · A0A060QNT8_9CAUD

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 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.

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 divalent metal cations per subunit. Mn2+ is preferred over Mg2+.

Features

Showing features for active site, binding site.

143250100150200250300350400
TypeIDPosition(s)Description
Active site142For ATPase activity
Binding site273Mn2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site273Mn2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site328Mn2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site405Mn2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site408Mn2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
    Endonuclease
  • EC number
  • Recommended name
    ATPase
  • EC number

Organism names

Accessions

  • Primary accession
    A0A060QNT8

Proteomes

Subcellular Location

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain32-238Phage terminase large subunit N-terminal
Motif39-46Walker A motif
Motif137-142Walker B motif
Domain273-415Phage terminase large subunit C-terminal

Domain

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    50,093
  • Last updated
    2014-09-03 v1
  • Checksum
    C12A5C448C01C3F2
MSQTYQIKQSDIVIDLPKTVGAGYGQFWRSRNLYRVVKGSRGSKKSKTTALNYVIRLLKYPWANLLVIRRYSNTNKQSTYTDFKWACNVLGVTHLFKFNESLPEITVKATGQKILFRGLDDELKITSITVDVGSLCWAWFEEAYQIETEDKFSTVVESIRGSLDVPDFFKQITVTFNPWNERHWLKRVFFDEETSRADTFATTTTYKCNEWLDEVDIKRYEDLYHTNPRRARIVCDGEWGVAEGLIYENVTVKDFDKDELLRDSANKLCIGLDFGFTHDPTALCCSLINDTTKEIYVFDEAYKVGLITKEVAKMIKDKGYHRSQIVADSAELRLIEELRSEHGITRIKESRKGKDSIMAGVSKLQGYAIYVHPDCKNIMDEFYSYCYQRDKEGNWLNKPEDKNNHLMDALRYSLQCIEGGKATVRRRSDYGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG799497
EMBL· GenBank· DDBJ
CDL74040.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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