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P16753

- SCAF_HCMVA

UniProt

P16753 - SCAF_HCMVA

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Protein

Capsid scaffolding protein

Gene

UL80

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).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).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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay system
Active sitei132 – 1321Charge relay system
Active sitei157 – 1571Charge relay system
Sitei256 – 2572Cleavage; by assemblin; Release site
Sitei643 – 6442Cleavage; by assemblin; Maturation site
Sitei675 – 6762Cleavage; by assemblin; Tail site

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Viral capsid assembly, Virus exit from host cell

Protein family/group databases

MEROPSiS21.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid scaffolding protein
Alternative name(s):
Capsid protein P40
Protease precursor
Short name:
pPR
Cleaved into the following 2 chains:
Alternative name(s):
Protease
Gene namesi
Name:UL80
Synonyms:APNG
OrganismiHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Taxonomic identifieri10360 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000008991: Genome, UP000008992: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Capsid scaffolding proteinPRO_0000027284Add
BLAST
Chaini1 – 256256AssemblinPRO_0000027285Add
BLAST
Chaini257 – 708452Assembly proteinBy similarityPRO_0000027286Add
BLAST

Post-translational modificationi

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).By similarity
Capsid assembly protein is phosphorylated.

Interactioni

Subunit structurei

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).By similarity

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Beta strandi14 – 229Combined sources
Helixi30 – 323Combined sources
Helixi36 – 427Combined sources
Beta strandi58 – 614Combined sources
Beta strandi64 – 7815Combined sources
Beta strandi81 – 888Combined sources
Helixi91 – 10111Combined sources
Helixi105 – 1084Combined sources
Beta strandi112 – 1154Combined sources
Helixi119 – 1279Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi172 – 1754Combined sources
Helixi177 – 1815Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 19911Combined sources
Helixi200 – 2045Combined sources
Helixi218 – 22912Combined sources
Helixi234 – 24411Combined sources
Helixi249 – 2513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP16753.
SMRiP16753. Positions 4-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16753.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni369 – 38820Interaction with pAPAdd
BLAST
Regioni688 – 70821Interaction with major capsid proteinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi510 – 5156Nuclear localization signal 1
Motifi537 – 5437Nuclear localization signal 2

Domaini

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).By similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.16.10. 1 hit.
InterProiIPR001847. Peptidase_S21.
[Graphical view]
PfamiPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSiPR00236. HSVCAPSIDP40.
SUPFAMiSSF50789. SSF50789. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative promoter usage. Align

Isoform Capsid scaffolding protein (identifier: P16753-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTMDEQQSQA VAPVYVGGFL ARYDQSPDEA ELLLPRDVVE HWLHAQGQGQ
60 70 80 90 100
PSLSVALPLN INHDDTAVVG HVAAMQSVRD GLFCLGCVTS PRFLEIVRRA
110 120 130 140 150
SEKSELVSRG PVSPLQPDKV VEFLSGSYAG LSLSSRRCDD VEAATSLSGS
160 170 180 190 200
ETTPFKHVAL CSVGRRRGTL AVYGRDPEWV TQRFPDLTAA DRDGLRAQWQ
210 220 230 240 250
RCGSTAVDAS GDPFRSDSYG LLGNSVDALY IRERLPKLRY DKQLVGVTER
260 270 280 290 300
ESYVKASVSP EAACDIKAAS AERSGDSRSQ AATPAAGARV PSSSPSPPVE
310 320 330 340 350
PPSPVQPPAL PASPSVLPAE SPPSLSPSEP AEAASMSHPL SAAVPAATAP
360 370 380 390 400
PGATVAGASP AVSSLAWPHD GVYLPKDAFF SLLGASRSAV PVMYPGAVAA
410 420 430 440 450
PPSASPAPLP LPSYPASYGA PVVGYDQLAA RHFADYVDPH YPGWGRRYEP
460 470 480 490 500
APSLHPSYPV PPPPSPAYYR RRDSPGGMDE PPSGWERYDG GHRGQSQKQH
510 520 530 540 550
RHGGSGGHNK RRKETAAASS SSSDEDLSFP GEAEHGRARK RLKSHVNSDG
560 570 580 590 600
GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPSAASS
610 620 630 640 650
SPTTTTVCTP TGELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA
660 670 680 690 700
SGSEAATAGP STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF

VAALNKLE
Length:708
Mass (Da):73,852
Last modified:August 1, 1990 - v1
Checksum:i32A993D6586824C9
GO
Isoform pAP (identifier: P16753-2) [UniParc]FASTAAdd to Basket

Also known as: Assembly protein, UL80.5

The sequence of this isoform differs from the canonical sequence as follows:
     1-335: Missing.

Show »
Length:373
Mass (Da):38,252
Checksum:iE98A2DA99A5E1597
GO
Isoform UL80.4 protein (identifier: P16753-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-392: Missing.

Show »
Length:316
Mass (Da):32,700
Checksum:i7E2E5EC4F9E51BF5
GO
Isoform UL80.3 protein (identifier: P16753-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:231
Mass (Da):23,601
Checksum:i19D7AC8C58798835
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 477477Missing in isoform UL80.3 protein. CuratedVSP_037425Add
BLAST
Alternative sequencei1 – 392392Missing in isoform UL80.4 protein. CuratedVSP_037424Add
BLAST
Alternative sequencei1 – 335335Missing in isoform pAP. CuratedVSP_037423Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS09843. QQBEB8.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S09843. QQBEB8.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CMV X-ray 2.27 A/B 1-256 [» ]
1ID4 X-ray 2.20 A/B 1-256 [» ]
1IEC X-ray 2.20 A/B 1-256 [» ]
1IED X-ray 2.00 A/B 1-256 [» ]
1IEF X-ray 2.30 A/B 1-256 [» ]
1IEG X-ray 2.00 A/B 1-256 [» ]
1JQ6 X-ray 2.30 A 1-256 [» ]
1JQ7 X-ray 3.00 A/B 1-256 [» ]
1LAY X-ray 2.50 A 1-256 [» ]
1NJT X-ray 2.50 A/B/C/D 1-256 [» ]
1NJU X-ray 2.70 A/B/C/D 1-256 [» ]
1NKK X-ray 2.60 A/B/C/D 1-256 [» ]
1NKM X-ray 2.70 A/B 1-256 [» ]
1WPO X-ray 2.00 A/B 1-256 [» ]
2WPO X-ray 2.70 A/B/C/D 1-256 [» ]
ProteinModelPortali P16753.
SMRi P16753. Positions 4-256.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P16753.
ChEMBLi CHEMBL3771.

Protein family/group databases

MEROPSi S21.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P16753.

Family and domain databases

Gene3Di 3.20.16.10. 1 hit.
InterProi IPR001847. Peptidase_S21.
[Graphical view ]
Pfami PF00716. Peptidase_S21. 1 hit.
[Graphical view ]
PRINTSi PR00236. HSVCAPSIDP40.
SUPFAMi SSF50789. SSF50789. 1 hit.
ProtoNeti Search...

Publicationsi

  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. Cited for: IDENTIFICATION.
  4. "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.
  5. "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.
  6. "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.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PROTEASE.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF PROTEASE.

Entry informationi

Entry nameiSCAF_HCMVA
AccessioniPrimary (citable) accession number: P16753
Secondary accession number(s): Q69030, Q7M6L0, Q7M6L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3