P12869 (CAPSD_BOOLV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Boolarra virus (BoV)

Taxonomic identifier

12286 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Nodaviridae › Alphanodavirus

Virus host

Hepialidae (ghost moths) [TaxID: 41021]

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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. 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 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 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
Biological process	Viral penetration into host cytoplasm Viral penetration via permeabilization of host organellar membrane Virus entry into host cell
Cellular component	Virion
Molecular function	Aspartyl protease Capsid protein Hydrolase Protease T=3 icosahedral capsid protein
PTM	Disulfide bond
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	T=3 icosahedral viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Capsid protein alpha		PRO_0000402387
	Chain	1 – 359	359	Capsid protein beta		PRO_0000039192
	Chain	360 – 403	44	Peptide gamma		PRO_0000039193
Regions
	Compositional bias	25 – 34	10	Poly-Arg
Sites
	Active site	61	1	By similarity
Amino acid modifications
	Disulfide bond	55 ↔ 314		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12869 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 73C3533D238B1EE9	FASTA	403	43,357
	10 20 30 40 50 60 MTPRRQQRPK GQLAKAKQAK QPLARSRRPR RRRRAAITQN NLMMLSEPGL SFLKCAFASP 70 80 90 100 110 120 DSNTDPGKGI PDNFEGKVLS QKNVYTETGV NFSGATTQNV DTYIIVLPTP GVAFWRCIKT 130 140 150 160 170 180 ATAPAQPAAL TTTDVFTAVP FPDFTSLFGT TATNRADQVA AFRYASMNFG LYPTCNSTQY 190 200 210 220 230 240 NGGISVWKGA VQMSTTQYPL DTTPESSQLV HAITGLESAL KVGDENYSES FIDGVFTQSI 250 260 270 280 290 300 NGNAEFPFYP ILEGVQTLPG QNVTVAQAGM PFSLDAGAAT VAGFTGIGGM DAIFIKVTAA 310 320 330 340 350 360 AGSVNTATIK TWACIEYRPN TNTALYKYAH DSPAEDIIAL QQYRKVYKSL PVAVRAKLNA 370 380 390 400 NMWERVKRLL KAGLVAASYV PGPVGGIATG VQHIGDLIAE LSF

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15960 Genomic RNA. Translation: CAA34082.1.
PIR	VCBBBL. A34011.
RefSeq	NP_689443.1. NC_004145.1.
3D structure databases
ProteinModelPortal	P12869.
SMR	P12869. Positions 42-359.
ModBase	Search...
Protein family/group databases
MEROPS	N01.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	956658.
Family and domain databases
InterPro	IPR000696. Peptidase_A6. [Graphical view]
Pfam	PF01829. Peptidase_A6. 1 hit. [Graphical view]
PRINTS	PR00863. NODAVIRPTASE.
ProtoNet	Search...

Entry information

Entry name

CAPSD_BOOLV

Accession

Primary (citable) accession number: P12869

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program