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Q9J7Z0

- CAPSD_PAV

UniProt

Q9J7Z0 - CAPSD_PAV

Protein

Capsid protein alpha

Gene

alpha

Organism
Pariacoto virus (PaV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma By similarity.By similarity
    Peptide gamma: membrane-permeabilizing peptide produced by virus maturation, thereby creating the infectious virion. After endocytosis into the host cell, peptide gamma is probably exposed in endosomes, where it permeabilizes the endosomal membrane, facilitating translocation of viral capsid or RNA into the cytoplasm By similarity.By similarity

    Catalytic activityi

    Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei68 – 681By similarity
    Metal bindingi249 – 2491Calcium
    Metal bindingi251 – 2511Calcium

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. permeabilization of host organelle membrane involved in viral entry into host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Keywords - Biological processi

    Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membrane, Virus entry into host cell

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Capsid protein alpha
    Cleaved into the following 2 chains:
    Alternative name(s):
    Coat protein beta
    Nodavirus endopeptidase
    Alternative name(s):
    Coat protein gamma
    Gene namesi
    Name:alpha
    OrganismiPariacoto virus (PaV)
    Taxonomic identifieri103782 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNodaviridaeAlphanodavirus
    Virus hostiSpodoptera eridania (Southern armyworm) [TaxID: 37547]

    Subcellular locationi

    Chain Peptide gamma : Virion Curated
    Note: located inside the capsid.Curated

    GO - Cellular componenti

    1. T=3 icosahedral viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, T=3 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Capsid protein alphaPRO_0000402390Add
    BLAST
    Chaini1 – 361361Capsid protein betaPRO_0000039198Add
    BLAST
    Chaini362 – 40140Peptide gammaPRO_0000039199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 316By similarity

    Post-translational modificationi

    Capsid protein alpha autocatalytically maturates into capsid protein beta and peptide gamma.By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni20 – 223
    Beta strandi46 – 483
    Helixi54 – 6411
    Beta strandi68 – 714
    Beta strandi83 – 9816
    Beta strandi100 – 1089
    Beta strandi114 – 1218
    Beta strandi129 – 1346
    Helixi138 – 1425
    Turni146 – 1494
    Turni151 – 1533
    Beta strandi155 – 17016
    Turni174 – 1763
    Beta strandi180 – 1867
    Beta strandi189 – 20012
    Beta strandi207 – 21812
    Helixi219 – 2213
    Beta strandi223 – 2253
    Beta strandi228 – 2347
    Helixi235 – 2373
    Beta strandi239 – 2424
    Beta strandi247 – 2493
    Beta strandi256 – 26611
    Beta strandi274 – 2763
    Helixi278 – 2814
    Beta strandi294 – 3018
    Beta strandi307 – 32115
    Helixi328 – 3303
    Helixi339 – 34810
    Helixi363 – 37412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F8VX-ray3.00A/B/C7-361[»]
    D/E/F362-401[»]
    ProteinModelPortaliQ9J7Z0.
    SMRiQ9J7Z0. Positions 7-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9J7Z0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A6 family.Curated

    Family and domain databases

    Gene3Di1.20.5.280. 1 hit.
    2.60.120.20. 1 hit.
    InterProiIPR023348. Pariacoto_capsid_alpha_C.
    IPR000696. Peptidase_A6.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF01829. Peptidase_A6. 1 hit.
    [Graphical view]
    PRINTSiPR00863. NODAVIRPTASE.

    Sequencei

    Sequence statusi: Complete.

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

    Q9J7Z0-1 [UniParc]FASTAAdd to Basket

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    MVSRTKNRRN KARKVVSRST ALVPMAPASQ RTGPAPRKPR KRNQALVRNP    50
    RLTDAGLAFL KCAFAAPDFS VDPGKGIPDN FHGRTLAIKD CNTTSVVFTP 100
    NTDTYIVVAP VPGFAYFRAE VAVGAQPTTF VGVPYPTYAT NFGAGSQNGL 150
    PAVNNYSKFR YASMACGLYP TSNMMQFSGS VQVWRVDLNL SEAVNPAVTA 200
    ITPAPGVFAN FVDKRINGLR GIRPLAPRDN YSGNFIDGAY TFAFDKSTDF 250
    EWCDFVRSLE FSESNVLGAA TAMKLLAPGG GTDTTLTGLG NVNTLVYKIS 300
    TPTGAVNTAI LRTWNCIELQ PYTDSALFQF SGVSPPFDPL ALECYHNLKM 350
    RFPVAVSSRE NSKFWEGVLR VLNQISGTLS VIPGPVGTIS AGVHQLTGMY 400
    M 401
    Length:401
    Mass (Da):43,326
    Last modified:October 1, 2000 - v1
    Checksum:i1E518977DE7A2C90
    GO

    Mass spectrometryi

    Molecular mass is 4246 Da from positions 362 - 401. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171943 Genomic RNA. Translation: AAF71693.1.
    RefSeqiNP_620111.1. NC_003692.1.

    Genome annotation databases

    GeneIDi956349.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171943 Genomic RNA. Translation: AAF71693.1 .
    RefSeqi NP_620111.1. NC_003692.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F8V X-ray 3.00 A/B/C 7-361 [» ]
    D/E/F 362-401 [» ]
    ProteinModelPortali Q9J7Z0.
    SMRi Q9J7Z0. Positions 7-361.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956349.

    Miscellaneous databases

    EvolutionaryTracei Q9J7Z0.

    Family and domain databases

    Gene3Di 1.20.5.280. 1 hit.
    2.60.120.20. 1 hit.
    InterProi IPR023348. Pariacoto_capsid_alpha_C.
    IPR000696. Peptidase_A6.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF01829. Peptidase_A6. 1 hit.
    [Graphical view ]
    PRINTSi PR00863. NODAVIRPTASE.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and construction of functional cDNA clones of Pariacoto virus, the first Alphanodavirus isolated outside Australasia."
      Johnson K.N., Zeddam J.-L., Ball L.A.
      J. Virol. 74:5123-5132(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], MASS SPECTROMETRY.
    2. "The structure of pariacoto virus reveals a dodecahedral cage of duplex RNA."
      Tang L., Johnson K.N., Ball L.A., Lin T., Yeager M., Johnson J.E.
      Nat. Struct. Biol. 8:77-83(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 7-401.

    Entry informationi

    Entry nameiCAPSD_PAV
    AccessioniPrimary (citable) accession number: Q9J7Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 77 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3