Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Capsid scaffolding protein

Gene

UL80

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed-Annotation score: 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 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 annotation
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 annotation
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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay systemUniRule annotation
Active sitei132 – 1321Charge relay systemUniRule annotation
Active sitei157 – 1571Charge relay systemUniRule annotation

GO - Molecular functioni

GO - Biological processi

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 proteinUniRule annotation
Alternative name(s):
Protease precursorUniRule annotation
Short name:
pPRUniRule annotation
Cleaved into the following 2 chains:
AssemblinUniRule annotation (EC:3.4.21.97UniRule annotation)
Alternative name(s):
ProteaseUniRule annotation
Assembly proteinUniRule annotation
Alternative name(s):
Capsid assembly proteinUniRule annotation
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]
Proteomesi
  • UP000008992 Componenti: Genome
  • UP000008991 Componenti: Genome

Subcellular locationi

Capsid scaffolding protein :
  • Host cytoplasm UniRule annotation
Assemblin :
  • Host nucleus UniRule annotation
Assembly protein :
  • Host nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Capsid scaffolding proteinPRO_0000027284Add
BLAST
Chaini1 – 256256AssemblinUniRule annotationPRO_0000027285Add
BLAST
Chaini257 – 708452Assembly proteinUniRule annotationPRO_0000027286Add
BLAST

Post-translational modificationi

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 and tail site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei256 – 2572Cleavage; by assemblin; Release siteUniRule annotation
Sitei643 – 6442Cleavage; by assemblin; Maturation site
Sitei684 – 6852Cleavage; by assemblin; Tail site

Keywords - PTMi

Phosphoprotein

Interactioni

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 annotation

Chemistry

BindingDBiP16753.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined 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
Regioni333 – 35220Interaction with pAPUniRule annotationAdd
BLAST
Regioni688 – 70821Interaction with major capsid proteinUniRule annotationAdd
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).UniRule annotation

Sequence similaritiesi

Belongs to the herpesviridae capsid scaffolding protein family.UniRule annotation

Family and domain databases

HAMAPiMF_04008. HSV_SCAF. 1 hit.
InterProiIPR001847. Peptidase_S21.
[Graphical view]
PfamiPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSiPR00236. HSVCAPSIDP40.

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. AlignAdd to basket

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 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.
PIRiS09843. QQBEB8.

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...

Chemistry

BindingDBiP16753.
ChEMBLiCHEMBL3771.

Protein family/group databases

MEROPSiS21.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP16753.

Family and domain databases

HAMAPiMF_04008. HSV_SCAF. 1 hit.
InterProiIPR001847. Peptidase_S21.
[Graphical view]
PfamiPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSiPR00236. HSVCAPSIDP40.
ProtoNetiSearch...

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: April 13, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.