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P12869

- CAPSD_BOOLV

UniProt

P12869 - CAPSD_BOOLV

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Protein
Capsid protein alpha
Gene
alpha
Organism
Boolarra virus (BoV)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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. 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: 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.

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 sitei61 – 611 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

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

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

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
OrganismiBoolarra virus (BoV)
Taxonomic identifieri12286 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNodaviridaeAlphanodavirus
Virus hostiHepialidae (ghost moths) [TaxID: 41021]

Subcellular locationi

Chain Capsid protein beta : Virion Reviewed prediction
Chain Peptide gamma : Virion Reviewed prediction
Note: Located inside the capsid and probably externalized in early endosomes Reviewed prediction.

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 – 403403Capsid protein alpha
PRO_0000402387Add
BLAST
Chaini1 – 359359Capsid protein beta
PRO_0000039192Add
BLAST
Chaini360 – 40344Peptide gamma
PRO_0000039193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 314 By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP12869.
SMRiP12869. Positions 42-359.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 3410Poly-Arg

Sequence similaritiesi

Belongs to the peptidase A6 family.

Family and domain databases

Gene3Di2.60.120.20. 1 hit.
InterProiIPR000696. 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.

P12869-1 [UniParc]FASTAAdd to Basket

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MTPRRQQRPK GQLAKAKQAK QPLARSRRPR RRRRAAITQN NLMMLSEPGL    50
SFLKCAFASP DSNTDPGKGI PDNFEGKVLS QKNVYTETGV NFSGATTQNV 100
DTYIIVLPTP GVAFWRCIKT ATAPAQPAAL TTTDVFTAVP FPDFTSLFGT 150
TATNRADQVA AFRYASMNFG LYPTCNSTQY NGGISVWKGA VQMSTTQYPL 200
DTTPESSQLV HAITGLESAL KVGDENYSES FIDGVFTQSI NGNAEFPFYP 250
ILEGVQTLPG QNVTVAQAGM PFSLDAGAAT VAGFTGIGGM DAIFIKVTAA 300
AGSVNTATIK TWACIEYRPN TNTALYKYAH DSPAEDIIAL QQYRKVYKSL 350
PVAVRAKLNA NMWERVKRLL KAGLVAASYV PGPVGGIATG VQHIGDLIAE 400
LSF 403
Length:403
Mass (Da):43,357
Last modified:October 1, 1989 - v1
Checksum:i73C3533D238B1EE9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15960 Genomic RNA. Translation: CAA34082.1.
PIRiA34011. VCBBBL.
RefSeqiNP_689443.1. NC_004145.1.

Genome annotation databases

GeneIDi956658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15960 Genomic RNA. Translation: CAA34082.1 .
PIRi A34011. VCBBBL.
RefSeqi NP_689443.1. NC_004145.1.

3D structure databases

ProteinModelPortali P12869.
SMRi P12869. Positions 42-359.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi N01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956658.

Family and domain databases

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

Publicationsi

  1. "Nucleotide sequences of three Nodavirus RNA2's: the messengers for their coat protein precursors."
    Dasgupta R., Sgro J.-Y.
    Nucleic Acids Res. 17:7525-7526(1989) [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: SIMILARITY TO OTHER NODAVIRUSES.

Entry informationi

Entry nameiCAPSD_BOOLV
AccessioniPrimary (citable) accession number: P12869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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