Q6SW62 · SCAF_HCMVM

Function

function

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.

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.

Catalytic activity

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site63Charge relay system
Active site132Charge relay system
Site143-144Cleavage; by assemblin; Internal site
Active site157Charge relay system
Site209-210Cleavage; by assemblin; Cryptic site
Site275-276Cleavage; by assemblin; Release site
Site643-644Cleavage; by assemblin; Maturation site

GO annotations

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

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Capsid scaffolding protein
  • Alternative names
    • Capsid protein P40
    • 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
    • Synonyms
      APNG

Organism names

Accessions

  • Primary accession
    Q6SW62
  • Secondary accessions
    • D2K3N8
    • D2K3N9
    • Q6SW61

Proteomes

Subcellular Location

Capsid scaffolding protein

Host cytoplasm

Assemblin

Host nucleus

Assembly protein

Host nucleus

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004182711-256Assemblin
ChainPRO_00004182701-708Capsid scaffolding protein
ChainPRO_0000418272257-708Assembly 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

Capsid scaffolding protein

Homomultimer. Interacts with major capsid protein.

Assemblin

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

Assembly protein

Homomultimer. Interacts with major capsid protein.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region270-339Disordered
Compositional bias273-290Polar residues
Compositional bias294-325Pro residues
Region333-352Interaction with pAP
Compositional bias455-469Pro residues
Region455-565Disordered
Motif510-515Nuclear localization signal 1
Compositional bias528-546Basic and acidic residues
Motif537-543Nuclear localization signal 2
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.

Keywords

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative promoter usage.

Q6SW62-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Capsid scaffolding protein
  • Synonyms
    pPR, UL80a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    708
  • Mass (Da)
    73,838
  • Last updated
    2004-07-05 v1
  • Checksum
    28106DF482DB0521
MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACVIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTSELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE

Q6SW62-2

  • Name
    pAP
  • Synonyms
    Assembly protein, UL80.5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q6SW62-3

  • Name
    UL80.4 protein
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q6SW62-4

  • Name
    UL80.3 protein
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAR31633.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0440191-335in isoform pAP
Alternative sequenceVSP_0440181-392in isoform UL80.4 protein
Alternative sequenceVSP_0440171-477in isoform UL80.3 protein
Compositional bias273-290Polar residues
Compositional bias294-325Pro residues
Compositional bias455-469Pro residues
Compositional bias528-546Basic and acidic residues
Compositional bias551-565Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY446894
EMBL· GenBank· DDBJ
AAR31632.1
EMBL· GenBank· DDBJ
Genomic DNA
AY446894
EMBL· GenBank· DDBJ
AAR31633.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp