Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P16753

- SCAF_HCMVA

UniProt

P16753 - SCAF_HCMVA

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell

    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 – 107
    Beta strandi14 – 229
    Helixi30 – 323
    Helixi36 – 427
    Beta strandi58 – 614
    Beta strandi64 – 7815
    Beta strandi81 – 888
    Helixi91 – 10111
    Helixi105 – 1084
    Beta strandi112 – 1154
    Helixi119 – 1279
    Beta strandi130 – 1334
    Beta strandi138 – 1403
    Beta strandi158 – 1636
    Beta strandi165 – 1684
    Beta strandi172 – 1754
    Helixi177 – 1815
    Beta strandi184 – 1863
    Helixi189 – 19911
    Helixi200 – 2045
    Helixi218 – 22912
    Helixi234 – 24411
    Helixi249 – 2513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTMDEQQSQA VAPVYVGGFL ARYDQSPDEA ELLLPRDVVE HWLHAQGQGQ    50
    PSLSVALPLN INHDDTAVVG HVAAMQSVRD GLFCLGCVTS PRFLEIVRRA 100
    SEKSELVSRG PVSPLQPDKV VEFLSGSYAG LSLSSRRCDD VEAATSLSGS 150
    ETTPFKHVAL CSVGRRRGTL AVYGRDPEWV TQRFPDLTAA DRDGLRAQWQ 200
    RCGSTAVDAS GDPFRSDSYG LLGNSVDALY IRERLPKLRY DKQLVGVTER 250
    ESYVKASVSP EAACDIKAAS AERSGDSRSQ AATPAAGARV PSSSPSPPVE 300
    PPSPVQPPAL PASPSVLPAE SPPSLSPSEP AEAASMSHPL SAAVPAATAP 350
    PGATVAGASP AVSSLAWPHD GVYLPKDAFF SLLGASRSAV PVMYPGAVAA 400
    PPSASPAPLP LPSYPASYGA PVVGYDQLAA RHFADYVDPH YPGWGRRYEP 450
    APSLHPSYPV PPPPSPAYYR RRDSPGGMDE PPSGWERYDG GHRGQSQKQH 500
    RHGGSGGHNK RRKETAAASS SSSDEDLSFP GEAEHGRARK RLKSHVNSDG 550
    GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPSAASS 600
    SPTTTTVCTP TGELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA 650
    SGSEAATAGP STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF 700
    VAALNKLE 708
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 98 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