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P04329 (CAPSD_BBV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Capsid protein alpha

Cleaved into the following 2 chains:

  1. Capsid protein beta
    EC=3.4.23.44
    Alternative name(s):
    Coat protein beta
    Nodavirus endopeptidase
  2. Peptide gamma
    Alternative name(s):
    Coat protein gamma
Gene names
Name:alpha
OrganismBlack beetle virus (BBV)
Taxonomic identifier12285 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNodaviridaeAlphanodavirus
Virus hostHeteronychus arator [TaxID: 295550]

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

Catalytic activity

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

Subcellular location

Capsid protein alpha: Virion Potential.

Capsid protein beta: Virion Potential.

Peptide gamma: Virion Potential. Note: Located inside the capsid and probably externalized in early endosomes Potential.

Post-translational modification

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

Sequence similarities

Belongs to the peptidase A6 family.

Ontologies

Keywords
   Cellular componentCapsid protein
T=3 icosahedral capsid protein
Virion
   LigandCalcium
Metal-binding
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentT=3 icosahedral viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Capsid protein alpha
PRO_0000402386
Chain1 – 363363Capsid protein beta
PRO_0000039190
Chain364 – 40744Peptide gamma
PRO_0000039191

Regions

Compositional bias17 – 226Poly-Thr
Compositional bias35 – 4612Poly-Arg

Sites

Active site751
Metal binding2491Calcium By similarity
Metal binding2511Calcium By similarity

Amino acid modifications

Disulfide bond69 ↔ 318 By similarity

Secondary structure

.......................................................... 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04329 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 3A6C6C9A98A5C26C

FASTA40743,838
        10         20         30         40         50         60 
MVRNNNRRRQ RTQRIVTTTT QTAPVPQQNV PKQPRRRRNR ARRNRRQGRA MNMGALTRLS 

        70         80         90        100        110        120 
QPGLAFLKCA FAPPDFNTDP GKGIPDRFEG KVVTRKDVLN QSINFTANRD TFILIAPTPG 

       130        140        150        160        170        180 
VAYWVADVPA GTFPISTTTF NAVNFPGFNS MFGNAAASRS DQVSSFRYAS MNVGIYPTSN 

       190        200        210        220        230        240 
LMQFAGSITV WKCPVKLSNV QFPVATTPAT SALVHTLVGL DGVLAVGPDN FSESFIKGVF 

       250        260        270        280        290        300 
SQSVCNEPDF EFSDILEGIQ TLPPANVTVA TSGQPFNLAA GAEAVSGIVG WGNMDTIVIR 

       310        320        330        340        350        360 
VSAPTGAVNS AILKTWACLE YRPNPNAMLY QFGHDSPPCD EVALQEYRTV ARSLPVAVIA 

       370        380        390        400 
AQNASMWERV KSIIKSSLAM ASNVPGPIGI AASGLSGLSA LFEGFGF 

« Hide

References

[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).

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00956 Genomic RNA. Translation: CAA25468.1.
PIRVCBB2G. A04151.
RefSeqNP_049329.1. NC_002037.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BBVX-ray2.80A/B/C1-363[»]
D/E/F364-407[»]
ProteinModelPortalP04329.
SMRP04329. Positions 20-363.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSN01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956653.

Family and domain databases

Gene3D2.60.120.20. 1 hit.
4.10.180.10. 1 hit.
InterProIPR027440. Capsid_prot_alpha-like_dom.
IPR000696. Peptidase_A6.
IPR029053. Viral_coat.
[Graphical view]
PfamPF01829. Peptidase_A6. 1 hit.
[Graphical view]
PRINTSPR00863. NODAVIRPTASE.
ProtoNetSearch...

Other

EvolutionaryTraceP04329.
PMAP-CutDBP04329.

Entry information

Entry nameCAPSD_BBV
AccessionPrimary (citable) accession number: P04329
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references