A0A126N917 · A0A126N917_HCMV
- ProteinCapsid scaffolding protein
- GeneUL80
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids708 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 63 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 132 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 157 | Charge relay system | ||||
Sequence: H | ||||||
Site | 256-257 | Cleavage; by assemblin; Release site | ||||
Sequence: AS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | host cell nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | nuclear capsid assembly | |
Biological Process | proteolysis | |
Biological Process | viral release from host cell |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCapsid scaffolding protein
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Betaherpesvirinae > Cytomegalovirus > Cytomegalovirus humanbeta5
- Virus hosts
Accessions
- Primary accessionA0A126N917
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023354679 | 1-256 | Assemblin | |||
Sequence: MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKA | ||||||
Chain | PRO_5023354680 | 1-708 | Capsid scaffolding protein | |||
Sequence: MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACDIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVPSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPAPYGAPVVGYDQLAARHFAEYVDPHYPGWGRRYEPAPPLHSACPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKEAAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAAWQSSTLLSAALPAAASSSPTTTTVCTPTGELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSETATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE | ||||||
Chain | PRO_5023354681 | 257-708 | Assembly protein | |||
Sequence: SVSPEAACDIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVPSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPAPYGAPVVGYDQLAARHFAEYVDPHYPGWGRRYEPAPPLHSACPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKEAAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAAWQSSTLLSAALPAAASSSPTTTTVCTPTGELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSETATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE |
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
- PTM
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
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 269-339 | Disordered | ||||
Sequence: ASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHP | ||||||
Compositional bias | 273-290 | Polar residues | ||||
Sequence: RSGDSRSQAATPAAGARV | ||||||
Compositional bias | 294-325 | Pro residues | ||||
Sequence: SPSPPVEPPSPVQPPALPASPSVLPAESPPSL | ||||||
Region | 464-565 | Disordered | ||||
Sequence: PSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKEAAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQR | ||||||
Compositional bias | 528-546 | Basic and acidic residues | ||||
Sequence: SFPGEAEHGRARKRLKSHV | ||||||
Compositional bias | 551-565 | Polar residues | ||||
Sequence: GSGGHAGSNQQQQQR | ||||||
Region | 688-708 | Interaction with major capsid protein | ||||
Sequence: PPKDMVDLNRRIFVAALNKLE |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length708
- Mass (Da)73,796
- Last updated2016-05-11 v1
- Checksum094464861F72235B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 273-290 | Polar residues | ||||
Sequence: RSGDSRSQAATPAAGARV | ||||||
Compositional bias | 294-325 | Pro residues | ||||
Sequence: SPSPPVEPPSPVQPPALPASPSVLPAESPPSL | ||||||
Compositional bias | 528-546 | Basic and acidic residues | ||||
Sequence: SFPGEAEHGRARKRLKSHV | ||||||
Compositional bias | 551-565 | Polar residues | ||||
Sequence: GSGGHAGSNQQQQQR |