CAPSD_BBV
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 03-AUG-2022, entry version 114.
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 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 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. In addition, calcium ions are
CC incorporated per capsid during assembly. The capsid encapsulates the
CC two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage
CC of capsid protein alpha generating capsid protein beta and the
CC membrane-active peptide gamma (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Peptide gamma is a membrane-disrupting peptide produced by
CC virus maturation, thereby creating the infectious virion. After
CC penetration into the host cell, peptide gamma is probably
CC exposed/released in endosomes, where it disrupts the endosomal
CC membrane, facilitating translocation of viral RNA into the cytoplasm
CC (By 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 alpha]: Virion {ECO:0000305}.
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}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2bbv";
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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 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.
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="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 BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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
