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P16753 (SCAF_HCMVA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Capsid scaffolding protein
Alternative name(s):
Capsid protein P40
Protease precursor
Short name=pPR

Cleaved into the following 2 chains:

  1. Assemblin
    EC=3.4.21.97
    Alternative name(s):
    Protease
  2. Assembly protein
Gene names
Name:UL80
Synonyms:APNG
OrganismHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) [Complete proteome]
Taxonomic identifier10360 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging By similarity.

Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging By similarity.

Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 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 By similarity.

Catalytic activity

Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.

Subunit structure

Capsid scaffolding protein homomultimerizes and interacts with major capsid protein UL86. Assemblin exists in a monomer-dimer equilibrium with the dimer being the active species. Assembly protein homomultimerizes and interacts with major capsid protein UL86 By similarity. Ref.6

Subcellular location

Capsid scaffolding protein: Host cytoplasm.

Assemblin: Host nucleus.

Assembly protein: Host nucleus.

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) By similarity.

Post-translational modification

Capsid scaffolding protein is cleaved by assemblin after completion of icosahedral capsid formation. Cleavages occur at two or more sites: release and tail site By similarity.

Capsid assembly protein is phosphorylated.

Sequence similarities

Belongs to the herpesviridae capsid scaffolding protein family.

Sequence caution

The sequence CAA35354.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processViral capsid assembly
Virus exit from host cell
   Cellular componentHost cytoplasm
Host nucleus
   Coding sequence diversityAlternative promoter usage
   Molecular functionHydrolase
Protease
Serine protease
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform Capsid scaffolding protein (identifier: P16753-1)

Also known as: pPR; UL80a;

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.
Isoform pAP (identifier: P16753-2)

Also known as: Assembly protein; UL80.5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-335: Missing.
Isoform UL80.4 protein (identifier: P16753-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-392: Missing.
Isoform UL80.3 protein (identifier: P16753-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-477: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Capsid scaffolding protein
PRO_0000027284
Chain1 – 256256Assemblin
PRO_0000027285
Chain257 – 708452Assembly protein By similarity
PRO_0000027286

Regions

Region369 – 38820Interaction with pAP
Region688 – 70821Interaction with major capsid protein
Motif510 – 5156Nuclear localization signal 1
Motif537 – 5437Nuclear localization signal 2

Sites

Active site631Charge relay system
Active site1321Charge relay system
Active site1571Charge relay system
Site256 – 2572Cleavage; by assemblin; Release site
Site643 – 6442Cleavage; by assemblin; Maturation site
Site675 – 6762Cleavage; by assemblin; Tail site

Natural variations

Alternative sequence1 – 477477Missing in isoform UL80.3 protein.
VSP_037425
Alternative sequence1 – 392392Missing in isoform UL80.4 protein.
VSP_037424
Alternative sequence1 – 335335Missing in isoform pAP.
VSP_037423

Secondary structure

.............................................. 708
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Capsid scaffolding protein (pPR) (UL80a) [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 32A993D6586824C9

FASTA70873,852
        10         20         30         40         50         60 
MTMDEQQSQA VAPVYVGGFL ARYDQSPDEA ELLLPRDVVE HWLHAQGQGQ PSLSVALPLN 

        70         80         90        100        110        120 
INHDDTAVVG HVAAMQSVRD GLFCLGCVTS PRFLEIVRRA SEKSELVSRG PVSPLQPDKV 

       130        140        150        160        170        180 
VEFLSGSYAG LSLSSRRCDD VEAATSLSGS ETTPFKHVAL CSVGRRRGTL AVYGRDPEWV 

       190        200        210        220        230        240 
TQRFPDLTAA DRDGLRAQWQ RCGSTAVDAS GDPFRSDSYG LLGNSVDALY IRERLPKLRY 

       250        260        270        280        290        300 
DKQLVGVTER ESYVKASVSP EAACDIKAAS AERSGDSRSQ AATPAAGARV PSSSPSPPVE 

       310        320        330        340        350        360 
PPSPVQPPAL PASPSVLPAE SPPSLSPSEP AEAASMSHPL SAAVPAATAP PGATVAGASP 

       370        380        390        400        410        420 
AVSSLAWPHD GVYLPKDAFF SLLGASRSAV PVMYPGAVAA PPSASPAPLP LPSYPASYGA 

       430        440        450        460        470        480 
PVVGYDQLAA RHFADYVDPH YPGWGRRYEP APSLHPSYPV PPPPSPAYYR RRDSPGGMDE 

       490        500        510        520        530        540 
PPSGWERYDG GHRGQSQKQH RHGGSGGHNK RRKETAAASS SSSDEDLSFP GEAEHGRARK 

       550        560        570        580        590        600 
RLKSHVNSDG GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPSAASS 

       610        620        630        640        650        660 
SPTTTTVCTP TGELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA SGSEAATAGP 

       670        680        690        700 
STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF VAALNKLE 

« Hide

Isoform pAP (Assembly protein) (UL80.5) [UniParc].

Checksum: E98A2DA99A5E1597
Show »

FASTA37338,252
Isoform UL80.4 protein [UniParc].

Checksum: 7E2E5EC4F9E51BF5
Show »

FASTA31632,700
Isoform UL80.3 protein [UniParc].

Checksum: 19D7AC8C58798835
Show »

FASTA23123,601

References

[1]"Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169."
Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R., Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A., Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.
Curr. Top. Microbiol. Immunol. 154:125-169(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The human cytomegalovirus genome revisited: comparison with the chimpanzee cytomegalovirus genome."
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., McGeoch D.J., Hayward G.S.
J. Gen. Virol. 84:17-28(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
[3]Erratum
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., McGeoch D.J., Hayward G.S.
J. Gen. Virol. 84:1053-1053(2003)
[4]"Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome."
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., Shenk T., Smith R.D., Nelson J.A.
J. Virol. 78:10960-10966(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[5]Erratum
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., Shenk T., Smith R.D., Nelson J.A.
J. Virol. 78:13395-13395(2004)
[6]"Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains."
Wood L.J., Baxter M.K., Plafker S.M., Gibson W.
J. Virol. 71:179-190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MULTIMERIZATION, INTERACTION WITH UL86.
[7]"Structure and formation of the cytomegalovirus virion."
Gibson W.
Curr. Top. Microbiol. Immunol. 325:187-204(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, ISOFORM UL80.4 PROTEIN AND UL80.3 PROTEIN.
[8]"A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease."
Tong L., Qian C., Massariol M.-J., Bonneau P.R., Cordingley M.G., Lagace L.
Nature 383:272-275(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PROTEASE.
[9]"Unique fold and active site in cytomegalovirus protease."
Qiu X., Culp J.S., Dilella A.G., Hellmig B., Hoog S.S., Janson C.A., Smith W.W., Abdel-Meguid S.A.
Nature 383:275-279(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PROTEASE.
[10]"Three-dimensional structure of human cytomegalovirus protease."
Shieh H.-S., Kurumbail R.G., Stevens A.M., Stegeman R.A., Sturman E.J., Pak J.Y., Wittwer A.J., Palmier M.O., Wiegand R.C., Holwerda B.C., Stallings W.C.
Nature 383:279-282(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF PROTEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17403 Genomic DNA. Translation: CAA35353.1.
X17403 Genomic DNA. Translation: CAA35354.1. Different initiation.
BK000394 Genomic DNA. Translation: DAA00177.1.
BK000394 Genomic DNA. Translation: DAA00178.1.
PIRQQBEB8. S09843.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMVX-ray2.27A/B1-256[»]
1ID4X-ray2.20A/B1-256[»]
1IECX-ray2.20A/B1-256[»]
1IEDX-ray2.00A/B1-256[»]
1IEFX-ray2.30A/B1-256[»]
1IEGX-ray2.00A/B1-256[»]
1JQ6X-ray2.30A1-256[»]
1JQ7X-ray3.00A/B1-256[»]
1LAYX-ray2.50A1-256[»]
1NJTX-ray2.50A/B/C/D1-256[»]
1NJUX-ray2.70A/B/C/D1-256[»]
1NKKX-ray2.60A/B/C/D1-256[»]
1NKMX-ray2.70A/B1-256[»]
1WPOX-ray2.00A/B1-256[»]
2WPOX-ray2.70A/B/C/D1-256[»]
ProteinModelPortalP16753.
SMRP16753. Positions 4-256.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP16753.
ChEMBLCHEMBL3771.

Protein family/group databases

MEROPSS21.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.16.10. 1 hit.
InterProIPR001847. Peptidase_S21.
[Graphical view]
PfamPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSPR00236. HSVCAPSIDP40.
SUPFAMSSF50789. SSF50789. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP16753.

Entry information

Entry nameSCAF_HCMVA
AccessionPrimary (citable) accession number: P16753
Secondary accession number(s): Q69030, Q7M6L0, Q7M6L1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references