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P04329

- CAPSD_BBV

UniProt

P04329 - CAPSD_BBV

Protein

Capsid protein alpha

Gene

alpha

Organism
Black beetle virus (BBV)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      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 is a membrane-disrupting peptide produced by virus maturation, thereby creating the infectious virion. After penetration into the host cell, peptide gamma is probably exposed/released in endosomes, where it disrupts the endosomal membrane, facilitating translocation of viral 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 sitei75 – 751
    Metal bindingi249 – 2491CalciumBy similarity
    Metal bindingi251 – 2511CalciumBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    MEROPSiN01.001.

    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
    OrganismiBlack beetle virus (BBV)
    Taxonomic identifieri12285 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNodaviridaeAlphanodavirus
    Virus hostiHeteronychus arator [TaxID: 295550]

    Subcellular locationi

    Chain Peptide gamma : Virion Curated
    Note: Located inside the capsid and probably externalized in early endosomes.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 – 407407Capsid protein alphaPRO_0000402386Add
    BLAST
    Chaini1 – 363363Capsid protein betaPRO_0000039190Add
    BLAST
    Chaini364 – 40744Peptide gammaPRO_0000039191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 ↔ 318By similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond

    Miscellaneous databases

    PMAP-CutDBP04329.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi61 – 7111
    Helixi73 – 753
    Beta strandi76 – 783
    Beta strandi90 – 10516
    Beta strandi109 – 1157
    Beta strandi121 – 1299
    Beta strandi139 – 1446
    Helixi148 – 1525
    Turni160 – 1623
    Beta strandi163 – 1697
    Beta strandi172 – 1776
    Turni181 – 1833
    Beta strandi187 – 1937
    Beta strandi196 – 2038
    Beta strandi211 – 2199
    Helixi220 – 2245
    Beta strandi231 – 2344
    Helixi235 – 2373
    Beta strandi239 – 2424
    Beta strandi247 – 2493
    Beta strandi260 – 2634
    Helixi269 – 2724
    Beta strandi275 – 2795
    Turni283 – 2853
    Beta strandi296 – 3038
    Beta strandi309 – 32315
    Beta strandi327 – 3293
    Helixi330 – 3323
    Helixi341 – 35212
    Helixi360 – 3623
    Helixi367 – 37610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BBVX-ray2.80A/B/C1-363[»]
    D/E/F364-407[»]
    ProteinModelPortaliP04329.
    SMRiP04329. Positions 20-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04329.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 226Poly-Thr
    Compositional biasi35 – 4612Poly-ArgAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase A6 family.Curated

    Family and domain databases

    Gene3Di2.60.120.20. 1 hit.
    4.10.180.10. 1 hit.
    InterProiIPR027440. Capsid_prot_alpha-like_dom.
    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.

    P04329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRNNNRRRQ RTQRIVTTTT QTAPVPQQNV PKQPRRRRNR ARRNRRQGRA    50
    MNMGALTRLS QPGLAFLKCA FAPPDFNTDP GKGIPDRFEG KVVTRKDVLN 100
    QSINFTANRD TFILIAPTPG VAYWVADVPA GTFPISTTTF NAVNFPGFNS 150
    MFGNAAASRS DQVSSFRYAS MNVGIYPTSN LMQFAGSITV WKCPVKLSNV 200
    QFPVATTPAT SALVHTLVGL DGVLAVGPDN FSESFIKGVF SQSVCNEPDF 250
    EFSDILEGIQ TLPPANVTVA TSGQPFNLAA GAEAVSGIVG WGNMDTIVIR 300
    VSAPTGAVNS AILKTWACLE YRPNPNAMLY QFGHDSPPCD EVALQEYRTV 350
    ARSLPVAVIA AQNASMWERV KSIIKSSLAM ASNVPGPIGI AASGLSGLSA 400
    LFEGFGF 407
    Length:407
    Mass (Da):43,838
    Last modified:March 20, 1987 - v1
    Checksum:i3A6C6C9A98A5C26C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00956 Genomic RNA. Translation: CAA25468.1.
    PIRiA04151. VCBB2G.
    RefSeqiNP_049329.1. NC_002037.1.

    Genome annotation databases

    GeneIDi956653.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00956 Genomic RNA. Translation: CAA25468.1 .
    PIRi A04151. VCBB2G.
    RefSeqi NP_049329.1. NC_002037.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BBV X-ray 2.80 A/B/C 1-363 [» ]
    D/E/F 364-407 [» ]
    ProteinModelPortali P04329.
    SMRi P04329. Positions 20-363.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi N01.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956653.

    Miscellaneous databases

    EvolutionaryTracei P04329.
    PMAP-CutDB P04329.

    Family and domain databases

    Gene3Di 2.60.120.20. 1 hit.
    4.10.180.10. 1 hit.
    InterProi IPR027440. Capsid_prot_alpha-like_dom.
    IPR000696. Peptidase_A6.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF01829. Peptidase_A6. 1 hit.
    [Graphical view ]
    PRINTSi PR00863. NODAVIRPTASE.
    ProtoNeti Search...

    Publicationsi

    1. "Primary and secondary structure of black beetle virus RNA2, the genomic messenger for BBV coat protein precursor."
      Dasgupta R., Ghosh A., Dasmahapatra B., Guarino L.A., Kaesberg P.
      Nucleic Acids Res. 12:7215-7223(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Structural homology among four nodaviruses as deduced by sequencing and X-ray crystallography."
      Kaesberg P., Dasgupta R., Sgro J.-Y., Wery J.-P., Selling B.H., Hosur M.V., Johnson J.E.
      J. Mol. Biol. 214:423-435(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, SIMILARITY TO OTHER NODAVIRUSES.
    3. "The refined three-dimensional structure of an insect virus at 2.8-A resolution."
      Wery J.-P., Reddy V.S., Hosur M.V., Johnson J.E.
      J. Mol. Biol. 235:565-586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiCAPSD_BBV
    AccessioniPrimary (citable) accession number: P04329
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 90 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