F5HEA7 · F5HEA7_HCMV

Function

function

Assemblin: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging.
Assembly protein: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.
Capsid scaffolding protein: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
    EC:3.4.21.97 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site63Charge relay system
Active site132Charge relay system
Active site157Charge relay system
Site256-257Cleavage; by assemblin; Release site

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componenthost cell nucleus
Molecular Functionidentical protein binding
Molecular Functionserine-type endopeptidase activity
Biological Processnuclear capsid assembly
Biological Processproteolysis
Biological Processviral release from host cell

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Capsid scaffolding protein
  • Alternative names
    • Protease precursor
      (pPR
      )
  • Cleaved into 2 chains
    • Assemblin
      (EC:3.4.21.97 (UniProtKB | ENZYME | Rhea)
      ) Alternative names: Protease
      (Pr
      )
    • Assembly protein
      (AP
      ) Alternative names: Capsid assembly protein

Gene names

    • Name
      UL80

Organism names

Accessions

  • Primary accession
    F5HEA7
  • Secondary accessions
    • A0A1D6WUN6

Proteomes

Subcellular Location

Capsid scaffolding protein

Host cytoplasm

Assembly protein

Host nucleus

Assemblin

Host nucleus

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50405499941-256Assemblin
ChainPRO_50405499961-708Capsid scaffolding protein
ChainPRO_5040549995257-708Assembly protein

Post-translational modification

Capsid scaffolding protein: Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release (R-site) and maturation (M-site).

Keywords

Interaction

Subunit

Assemblin

Exists in a monomer-dimer equilibrium with the dimer being the active species.

Assembly protein

Homomultimer. Interacts with major capsid protein.

Capsid scaffolding protein

Homomultimer. Interacts with major capsid protein.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region270-339Disordered
Compositional bias273-290Polar residues
Compositional bias294-325Pro residues
Compositional bias455-469Pro residues
Region455-565Disordered
Compositional bias528-546Basic and acidic residues
Compositional bias551-565Polar residues
Region593-620Disordered
Region688-708Interaction with major capsid protein

Domain

Region of interaction between pPR and pAP is called Amino conserved domain (ACD). The region of interaction with major capsid protein is called carboxyl conserved domain (CCD).

Sequence similarities

Belongs to the herpesviridae capsid scaffolding protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    708
  • Mass (Da)
    73,838
  • Last updated
    2011-06-28 v1
  • Checksum
    28106DF482DB0521
MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACVIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTSELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias273-290Polar residues
Compositional bias294-325Pro residues
Compositional bias455-469Pro residues
Compositional bias528-546Basic and acidic residues
Compositional bias551-565Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GU179001
EMBL· GenBank· DDBJ
ACZ72823.1
EMBL· GenBank· DDBJ
Genomic DNA
KM192298
EMBL· GenBank· DDBJ
AII79514.1
EMBL· GenBank· DDBJ
Genomic DNA
KM192299
EMBL· GenBank· DDBJ
AII79682.1
EMBL· GenBank· DDBJ
Genomic DNA
KM192300
EMBL· GenBank· DDBJ
AII79847.1
EMBL· GenBank· DDBJ
Genomic DNA
KM192301
EMBL· GenBank· DDBJ
AII80006.1
EMBL· GenBank· DDBJ
Genomic DNA
KM192302
EMBL· GenBank· DDBJ
AII80173.1
EMBL· GenBank· DDBJ
Genomic DNA
KP745662
EMBL· GenBank· DDBJ
AKI12476.1
EMBL· GenBank· DDBJ
Genomic DNA
KT726952
EMBL· GenBank· DDBJ
AMJ54609.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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