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P04329

- CAPSD_BBV

UniProt

P04329 - CAPSD_BBV

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Protein

Capsid protein alpha

Gene

alpha

Organism
Black beetle virus (BBV)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 7111Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 783Combined sources
Beta strandi90 – 10516Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi121 – 1299Combined sources
Beta strandi139 – 1446Combined sources
Helixi148 – 1525Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi172 – 1776Combined sources
Turni181 – 1833Combined sources
Beta strandi187 – 1937Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi211 – 2199Combined sources
Helixi220 – 2245Combined sources
Beta strandi231 – 2344Combined sources
Helixi235 – 2373Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi260 – 2634Combined sources
Helixi269 – 2724Combined sources
Beta strandi275 – 2795Combined sources
Turni283 – 2853Combined sources
Beta strandi296 – 3038Combined sources
Beta strandi309 – 32315Combined sources
Beta strandi327 – 3293Combined sources
Helixi330 – 3323Combined sources
Helixi341 – 35212Combined sources
Helixi360 – 3623Combined sources
Helixi367 – 37610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVRNNNRRRQ RTQRIVTTTT QTAPVPQQNV PKQPRRRRNR ARRNRRQGRA
60 70 80 90 100
MNMGALTRLS QPGLAFLKCA FAPPDFNTDP GKGIPDRFEG KVVTRKDVLN
110 120 130 140 150
QSINFTANRD TFILIAPTPG VAYWVADVPA GTFPISTTTF NAVNFPGFNS
160 170 180 190 200
MFGNAAASRS DQVSSFRYAS MNVGIYPTSN LMQFAGSITV WKCPVKLSNV
210 220 230 240 250
QFPVATTPAT SALVHTLVGL DGVLAVGPDN FSESFIKGVF SQSVCNEPDF
260 270 280 290 300
EFSDILEGIQ TLPPANVTVA TSGQPFNLAA GAEAVSGIVG WGNMDTIVIR
310 320 330 340 350
VSAPTGAVNS AILKTWACLE YRPNPNAMLY QFGHDSPPCD EVALQEYRTV
360 370 380 390 400
ARSLPVAVIA AQNASMWERV KSIIKSSLAM ASNVPGPIGI AASGLSGLSA

LFEGFGF
Length:407
Mass (Da):43,838
Last modified:March 20, 1987 - v1
Checksum:i3A6C6C9A98A5C26C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 91 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