ID CAPSD_BBV Reviewed; 407 AA. AC P04329; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 28-JUN-2023, entry version 116. 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 Black beetle virus (BBV). OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Magsaviricetes; OC Nodamuvirales; Nodaviridae; Alphanodavirus. OX NCBI_TaxID=12285; OH NCBI_TaxID=295550; Heteronychus arator (African black beetle). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=6548308; DOI=10.1093/nar/12.18.7215; RA Dasgupta R., Ghosh A., Dasmahapatra B., Guarino L.A., Kaesberg P.; RT "Primary and secondary structure of black beetle virus RNA2, the genomic RT messenger for BBV coat protein precursor."; RL Nucleic Acids Res. 12:7215-7223(1984). RN [2] RP CRYSTALLIZATION, AND 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). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=8289282; DOI=10.1006/jmbi.1994.1014; RA Wery J.-P., Reddy V.S., Hosur M.V., Johnson J.E.; RT "The refined three-dimensional structure of an insect virus at 2.8-A RT resolution."; RL J. Mol. Biol. 235:565-586(1994). 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 alpha]: Virion {ECO:0000305}. 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 -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid CC structure; CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2bbv"; 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; X00956; CAA25468.1; -; Genomic_RNA. DR PIR; A04151; VCBB2G. DR RefSeq; NP_049329.1; NC_002037.1. DR PDB; 2BBV; X-ray; 2.80 A; A/B/C=1-363, D/E/F=364-407. DR PDBsum; 2BBV; -. DR SMR; P04329; -. DR MEROPS; N01.001; -. DR GeneID; 956653; -. DR KEGG; vg:956653; -. DR OrthoDB; 10195at10239; -. DR EvolutionaryTrace; P04329; -. DR Proteomes; UP000203003; 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:0006508; P:proteolysis; 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 1: Evidence at protein level; KW 3D-structure; Aspartyl protease; Calcium; Capsid protein; Disulfide bond; KW Hydrolase; Metal-binding; Protease; T=3 icosahedral capsid protein; Virion. FT CHAIN 1..407 FT /note="Capsid protein alpha" FT /id="PRO_0000402386" FT CHAIN 1..363 FT /note="Capsid protein beta" FT /id="PRO_0000039190" FT CHAIN 364..407 FT /note="Membrane-lytic peptide gamma" FT /id="PRO_0000039191" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..47 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 75 FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 249 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12870" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P12870" FT SITE 363..364 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P12870" FT DISULFID 69..318 FT /evidence="ECO:0000250" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 90..105 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 148..152 FT /evidence="ECO:0007829|PDB:2BBV" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 172..177 FT /evidence="ECO:0007829|PDB:2BBV" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 220..224 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:2BBV" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 296..303 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 309..323 FT /evidence="ECO:0007829|PDB:2BBV" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 341..352 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:2BBV" FT HELIX 367..376 FT /evidence="ECO:0007829|PDB:2BBV" SQ SEQUENCE 407 AA; 43838 MW; 3A6C6C9A98A5C26C CRC64; MVRNNNRRRQ RTQRIVTTTT QTAPVPQQNV PKQPRRRRNR ARRNRRQGRA MNMGALTRLS QPGLAFLKCA FAPPDFNTDP GKGIPDRFEG KVVTRKDVLN QSINFTANRD TFILIAPTPG VAYWVADVPA GTFPISTTTF NAVNFPGFNS MFGNAAASRS DQVSSFRYAS MNVGIYPTSN LMQFAGSITV WKCPVKLSNV QFPVATTPAT SALVHTLVGL DGVLAVGPDN FSESFIKGVF SQSVCNEPDF EFSDILEGIQ TLPPANVTVA TSGQPFNLAA GAEAVSGIVG WGNMDTIVIR VSAPTGAVNS AILKTWACLE YRPNPNAMLY QFGHDSPPCD EVALQEYRTV ARSLPVAVIA AQNASMWERV KSIIKSSLAM ASNVPGPIGI AASGLSGLSA LFEGFGF //