ID   CAPSD_BOOLV             Reviewed;         403 AA.
AC   P12869;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Capsid protein alpha;
DE   Contains:
DE     RecName: Full=Capsid protein beta;
DE              EC=3.4.23.44;
DE     AltName: Full=Coat protein beta;
DE     AltName: Full=Nodavirus endopeptidase;
DE   Contains:
DE     RecName: Full=Peptide gamma;
DE     AltName: Full=Coat protein gamma;
GN   Name=alpha;
OS   Boolarra virus (BoV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Magsaviricetes;
OC   Nodamuvirales; Nodaviridae; Alphanodavirus.
OX   NCBI_TaxID=12286;
OH   NCBI_TaxID=41021; Hepialidae (ghost moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2798110; DOI=10.1093/nar/17.18.7525;
RA   Dasgupta R., Sgro J.-Y.;
RT   "Nucleotide sequences of three Nodavirus RNA2's: the messengers for their
RT   coat protein precursors.";
RL   Nucleic Acids Res. 17:7525-7526(1989).
RN   [2]
RP   SIMILARITY TO OTHER NODAVIRUSES.
RX   PubMed=2116525; DOI=10.1016/0022-2836(90)90191-n;
RA   Kaesberg P., Dasgupta R., Sgro J.-Y., Wery J.-P., Selling B.H., Hosur M.V.,
RA   Johnson J.E.;
RT   "Structural homology among four nodaviruses as deduced by sequencing and X-
RT   ray crystallography.";
RL   J. Mol. Biol. 214:423-435(1990).
CC   -!- FUNCTION: Capsid protein alpha self-assembles to form an icosahedral
CC       procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting
CC       of 60 capsid proteins trimers. The capsid encapsulates the two genomic
CC       RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid
CC       protein alpha generating capsid protein beta and the membrane-active
CC       peptide gamma (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Peptide gamma]: Membrane-permeabilizing peptide produced by
CC       virus maturation, thereby creating the infectious virion. After
CC       endocytosis into the host cell, peptide gamma is probably exposed in
CC       endosomes, where it permeabilizes the endosomal membrane, facilitating
CC       translocation of viral capsid or RNA into the cytoplasm (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of an asparaginyl bond involved in the maturation
CC         of the structural protein of the virus, typically -Asn-|-Ala- or
CC         -Asn-|-Phe-.; EC=3.4.23.44;
CC   -!- SUBCELLULAR LOCATION: [Capsid protein beta]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Peptide gamma]: Virion {ECO:0000305}.
CC       Note=Located inside the capsid and probably externalized in early
CC       endosomes. {ECO:0000305}.
CC   -!- PTM: Capsid protein alpha autocatalytically maturates into capsid
CC       protein beta and peptide gamma. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A6 family. {ECO:0000305}.
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DR   EMBL; X15960; CAA34082.1; -; Genomic_RNA.
DR   PIR; A34011; VCBBBL.
DR   RefSeq; NP_689443.1; NC_004145.1.
DR   SMR; P12869; -.
DR   MEROPS; N01.001; -.
DR   GeneID; 956658; -.
DR   KEGG; vg:956658; -.
DR   Proteomes; UP000204043; Genome.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR000696; Peptidase_A6.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF01829; Peptidase_A6; 1.
DR   PRINTS; PR00863; NODAVIRPTASE.
PE   3: Inferred from homology;
KW   Aspartyl protease; Capsid protein; Disulfide bond; Hydrolase; Protease;
KW   T=3 icosahedral capsid protein; Viral penetration into host cytoplasm;
KW   Viral penetration via permeabilization of host membrane; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..403
FT                   /note="Capsid protein alpha"
FT                   /id="PRO_0000402387"
FT   CHAIN           1..359
FT                   /note="Capsid protein beta"
FT                   /id="PRO_0000039192"
FT   CHAIN           360..403
FT                   /note="Peptide gamma"
FT                   /id="PRO_0000039193"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..314
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  43357 MW;  73C3533D238B1EE9 CRC64;
     MTPRRQQRPK GQLAKAKQAK QPLARSRRPR RRRRAAITQN NLMMLSEPGL SFLKCAFASP
     DSNTDPGKGI PDNFEGKVLS QKNVYTETGV NFSGATTQNV DTYIIVLPTP GVAFWRCIKT
     ATAPAQPAAL TTTDVFTAVP FPDFTSLFGT TATNRADQVA AFRYASMNFG LYPTCNSTQY
     NGGISVWKGA VQMSTTQYPL DTTPESSQLV HAITGLESAL KVGDENYSES FIDGVFTQSI
     NGNAEFPFYP ILEGVQTLPG QNVTVAQAGM PFSLDAGAAT VAGFTGIGGM DAIFIKVTAA
     AGSVNTATIK TWACIEYRPN TNTALYKYAH DSPAEDIIAL QQYRKVYKSL PVAVRAKLNA
     NMWERVKRLL KAGLVAASYV PGPVGGIATG VQHIGDLIAE LSF