UniProtKB - O40922 (O40922_HHV8)
Capsid scaffolding protein
ORF17
Functioni
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.
UniRule annotationAssembly 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.
UniRule annotationCapsid 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.
UniRule annotationCaution
Catalytic activityi
- Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.UniRule annotation EC:3.4.21.97
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 65 | Charge relay systemUniRule annotation | 1 | |
Active sitei | 133 | Charge relay systemUniRule annotation | 1 | |
Active sitei | 153 | Charge relay systemUniRule annotation | 1 |
GO - Molecular functioni
- identical protein binding Source: UniProtKB-UniRule
- serine-type endopeptidase activity Source: UniProtKB-UniRule
GO - Biological processi
- viral release from host cell Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase, Protease, Serine proteaseUniRule annotation |
Biological process | Viral capsid assemblyUniRule annotationARBA annotation, Viral release from host cell |
Protein family/group databases
MEROPSi | S21.006 |
Names & Taxonomyi
Protein namesi | Recommended name: Capsid scaffolding proteinUniRule annotationAlternative name(s): Protease precursorUniRule annotation Short name: pPRUniRule annotation Cleaved into the following 2 chains: Alternative name(s): ProteaseUniRule annotation Assembly proteinUniRule annotation Alternative name(s): Capsid assembly proteinUniRule annotation |
Gene namesi | Name:ORF17Imported |
Organismi | Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)Imported |
Taxonomic identifieri | 37296 [NCBI] |
Taxonomic lineagei | Viruses › Duplodnaviria › Heunggongvirae › Peploviricota › Herviviricetes › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Rhadinovirus |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
Other locations
- Host cytoplasm UniRule annotation
Other locations
- Host nucleus UniRule annotation
Other locations
- Host nucleus UniRule annotation
Other locations
- host cell cytoplasm Source: UniProtKB-SubCell
- host cell nucleus Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cytoplasmUniRule annotationARBA annotation, Host nucleusUniRule annotationPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_5033148626 | 1 – 553 | Capsid scaffolding proteinUniRule annotationAdd BLAST | 553 | |
ChainiPRO_5033148627 | 1 – 249 | AssemblinUniRule annotationAdd BLAST | 249 | |
ChainiPRO_5033148628 | 250 – 553 | Assembly proteinUniRule annotationAdd BLAST | 304 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 249 – 250 | Cleavage; by assemblin; Release siteUniRule annotation | 2 |
Keywords - PTMi
PhosphoproteinUniRule annotationARBA annotationInteractioni
Subunit structurei
Capsid scaffolding protein homomultimerizes and interacts with major capsid protein. Assemblin exists in a monomer-dimer equilibrium with the dimer being the active species. Assembly protein homomultimerizes and interacts with major capsid protein.
UniRule annotationGO - Molecular functioni
- identical protein binding Source: UniProtKB-UniRule
Structurei
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 356 – 375 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 485 – 543 | DisorderedSequence analysisAdd BLAST | 59 | |
Regioni | 533 – 553 | Interaction with major capsid proteinUniRule annotationAdd BLAST | 21 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 382 – 402 | Sequence analysisAdd BLAST | 21 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 357 – 375 | Basic and acidic residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 491 – 509 | Polar residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 520 – 534 | Polar residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coilSequence analysisFamily and domain databases
Gene3Di | 3.20.16.10, 1 hit |
HAMAPi | MF_04008, HSV_SCAF, 1 hit |
InterProi | View protein in InterPro IPR035443, Herpes_virus_sf IPR001847, Peptidase_S21 |
Pfami | View protein in Pfam PF00716, Peptidase_S21, 1 hit |
PRINTSi | PR00236, HSVCAPSIDP40 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MSLLSPGLSG SVSHTYFPSM AQGLYVGGFV DVVSCPKLEQ ELYLDPDQVT
60 70 80 90 100
DYLPVTEPLP ITIEHLPETE VGWTLGLFQV SHGIFCTGAI TSPAFLELAS
110 120 130 140 150
RLADTSHVAR APVKNLPKEP LLEILHTWLP GLSLSSIHPR ELSQTPSGPV
160 170 180 190 200
FQHVSLCALG RRRGTVAVYG HDAEWVVSRF SSVSKSERAH ILQHVSSCRL
210 220 230 240 250
EDLSTPNFVS PLETLMAKAI DASFIRDRLD LLKTDRGVAS ILSPAYLKAS
260 270 280 290 300
QFPVGIQAVT PPRPAMNSSG QEDIISIPKS AFLSMLQSSI DGMKTTAAKM
310 320 330 340 350
SHTLSGPGLM GCGGQMFPTD HHLPSYVSNP APPYGYAYKN PYDPWYYSPQ
360 370 380 390 400
LPGYRTGKRK RGAEDDEGHL FPGEEPAYHK DILSMSKNIA EIQSELKEMK
410 420 430 440 450
LNGWHAGPPP SSSAAAAAVD PHYRPHANSA APCQFPTMKE HGGTYVHPPI
460 470 480 490 500
YVQAPHGQFQ QAAPILFAQP HVSHPPVSTG LAVVGAPPAE PTPASSTQSI
510 520 530 540 550
QQQAPETTHT PCAAVEKDAP TPNPTSNRVE ASSRSSPKSK IRKMFCEELL
NKQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U93872 Genomic DNA Translation: AAB62670.1 GQ994935 Genomic DNA Translation: ACY00414.1 JQ619843 Genomic DNA Translation: AFU08284.1 KF588566 Genomic DNA Translation: AKE33052.1 AP017458 Genomic DNA Translation: BAV17867.1 MK143395 Genomic DNA Translation: QAX88081.1 MK876733 Genomic DNA Translation: QKE51343.1 MK876737 Genomic DNA Translation: QKE51691.1 MK876738 Genomic DNA Translation: QKE51778.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U93872 Genomic DNA Translation: AAB62670.1 GQ994935 Genomic DNA Translation: ACY00414.1 JQ619843 Genomic DNA Translation: AFU08284.1 KF588566 Genomic DNA Translation: AKE33052.1 AP017458 Genomic DNA Translation: BAV17867.1 MK143395 Genomic DNA Translation: QAX88081.1 MK876733 Genomic DNA Translation: QKE51343.1 MK876737 Genomic DNA Translation: QKE51691.1 MK876738 Genomic DNA Translation: QKE51778.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5UR3 | X-ray | 1.80 | A/B | 23-215 | [»] | |
5UTE | X-ray | 2.05 | A/B | 23-215 | [»] | |
5UTN | X-ray | 1.80 | A/B | 23-215 | [»] | |
5UV3 | X-ray | 1.95 | A/B | 23-215 | [»] | |
5UVP | X-ray | 1.94 | A/B | 23-215 | [»] | |
5V5D | X-ray | 2.10 | A/B | 23-215 | [»] | |
5V5E | X-ray | 2.30 | A/B | 23-215 | [»] | |
ModBasei | Search... | |||||
SWISS-MODEL-Workspacei | Submit a new modelling project... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | S21.006 |
Family and domain databases
Gene3Di | 3.20.16.10, 1 hit |
HAMAPi | MF_04008, HSV_SCAF, 1 hit |
InterProi | View protein in InterPro IPR035443, Herpes_virus_sf IPR001847, Peptidase_S21 |
Pfami | View protein in Pfam PF00716, Peptidase_S21, 1 hit |
PRINTSi | PR00236, HSVCAPSIDP40 |
MobiDBi | Search... |
Entry informationi
Entry namei | O40922_HHV8 | |
Accessioni | O40922Primary (citable) accession number: O40922 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | January 1, 1998 |
Last sequence update: | January 1, 1998 | |
Last modified: | January 19, 2022 | |
This is version 92 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |