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 13-SEP-2023, entry version 105. DE RecName: Full=Capsid protein alpha; DE EC=3.4.23.44 {ECO:0000250|UniProtKB:P12870}; DE Contains: DE RecName: Full=Capsid protein beta; DE AltName: Full=Coat protein beta; DE AltName: Full=Nodavirus endopeptidase; DE Contains: DE RecName: Full=Membrane-lytic 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]: Capsid protein alpha self-assembles CC to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in CC diameter, and consisting of 60 capsid proteins trimers. In addition, CC 240 calcium ions are incorporated per capsid during assembly. The CC capsid encapsulates the two genomic RNAs. Capsid maturation occurs via CC autoproteolytic cleavage of capsid protein alpha generating capsid CC protein beta and the membrane-active peptide gamma. CC {ECO:0000250|UniProtKB:P12870}. CC -!- FUNCTION: [Membrane-lytic peptide gamma]: Membrane-permeabilizing CC peptide produced by virus maturation, thereby creating the infectious CC virion. After endocytosis into the host cell, peptide gamma is probably CC exposed in endosomes, where it permeabilizes the endosomal membrane, CC facilitating translocation of viral capsid or RNA into the cytoplasm. CC Involved in specific recognition and packaging of viral RNA during CC assembly. {ECO:0000250|UniProtKB:P12870}. CC -!- CATALYTIC ACTIVITY: [Capsid protein beta]: 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; Evidence={ECO:0000250|UniProtKB:P12870}; CC -!- SUBCELLULAR LOCATION: [Capsid protein beta]: Virion {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Membrane-lytic peptide gamma]: Virion CC {ECO:0000305}. Note=Located inside the capsid and probably externalized CC in early endosomes. {ECO:0000305}. CC -!- PTM: [Capsid protein alpha]: Capsid protein alpha autocatalytically CC maturates into capsid protein beta and peptide gamma. CC {ECO:0000250|UniProtKB:P12870}. CC -!- SIMILARITY: Belongs to the peptidase A6 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OrthoDB; 10195at10239; -. 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:0046872; F:metal ion binding; 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. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1. PE 3: Inferred from homology; KW Aspartyl protease; Calcium; Capsid protein; Disulfide bond; Hydrolase; KW Metal-binding; Protease; T=3 icosahedral capsid protein; KW 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="Membrane-lytic 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|UniProtKB:P12870" FT BINDING 157 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 157 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 157 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 245 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P12870" FT SITE 359..360 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P12870" 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 //