CAPSD_FHV
ID CAPSD_FHV Reviewed; 407 AA.
AC P12870;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Flock house virus (FHV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Magsaviricetes;
OC Nodamuvirales; Nodaviridae; Alphanodavirus.
OX NCBI_TaxID=12287;
OH NCBI_TaxID=50579; Costelytra zealandica.
OH NCBI_TaxID=7137; Galleria mellonella (Greater wax moth).
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast).
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).
RN [3]
RP FUNCTION OF PEPTIDE GAMMA.
RX PubMed=9765417; DOI=10.1128/jvi.72.11.8738-8746.1998;
RA Schneemann A., Marshall D.;
RT "Specific encapsidation of nodavirus RNAs is mediated through the C
RT terminus of capsid precursor protein alpha.";
RL J. Virol. 72:8738-8746(1998).
RN [4]
RP FUNCTION OF PEPTIDE GAMMA, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=19553341; DOI=10.1128/jvi.00873-09;
RA Odegard A.L., Kwan M.H., Walukiewicz H.E., Banerjee M., Schneemann A.,
RA Johnson J.E.;
RT "Low endocytic pH and capsid protein autocleavage are critical components
RT of Flock House virus cell entry.";
RL J. Virol. 83:8628-8637(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=8421524; DOI=10.1038/361176a0;
RA Fisher A.J., Johnson J.E.;
RT "Ordered duplex RNA controls capsid architecture in an icosahedral animal
RT virus.";
RL Nature 361:176-179(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS), AND FUNCTION.
RX PubMed=20164221; DOI=10.1128/jvi.02670-09;
RA Banerjee M., Speir J.A., Kwan M.H., Huang R., Aryanpur P.P., Bothner B.,
RA Johnson J.E.;
RT "Structure and function of a genetically engineered mimic of a nonenveloped
RT virus entry intermediate.";
RL J. Virol. 84:4737-4746(2010).
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, 240 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.
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 (Probable).
CC {ECO:0000305}.
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.
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=fhv";
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; X15959; CAA34081.1; -; Genomic_RNA.
DR PIR; B34011; VCBBFH.
DR RefSeq; NP_689442.1; NC_004144.1.
DR PDB; 3LOB; X-ray; 3.60 A; A/B/C=1-363, D/E/F=364-407.
DR PDB; 4FSJ; X-ray; 3.50 A; A/B/C=1-363, D/E/F=364-407.
DR PDB; 4FTB; X-ray; 2.70 A; A/B/C=1-363, D/E/F=364-407.
DR PDB; 4FTE; X-ray; 3.50 A; A/B/C=1-407.
DR PDB; 4FTS; X-ray; 3.20 A; A/B/C=1-407.
DR PDB; 6ITB; EM; 4.70 A; A/B/C=1-363.
DR PDB; 6ITF; EM; 4.70 A; A/B/C=1-363.
DR PDBsum; 3LOB; -.
DR PDBsum; 4FSJ; -.
DR PDBsum; 4FTB; -.
DR PDBsum; 4FTE; -.
DR PDBsum; 4FTS; -.
DR PDBsum; 6ITB; -.
DR PDBsum; 6ITF; -.
DR SMR; P12870; -.
DR MEROPS; N01.001; -.
DR TCDB; 1.A.61.1.2; the insect nodavirus channel-forming chain f (gamma-peptide) family.
DR GeneID; 962115; -.
DR KEGG; vg:962115; -.
DR EvolutionaryTrace; P12870; -.
DR Proteomes; UP000203899; 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.
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;
KW Viral penetration into host cytoplasm;
KW Viral penetration via permeabilization of host membrane; Virion;
KW Virus entry into host cell.
FT CHAIN 1..407
FT /note="Capsid protein alpha"
FT /id="PRO_0000402388"
FT CHAIN 1..363
FT /note="Capsid protein beta"
FT /id="PRO_0000039194"
FT CHAIN 364..407
FT /note="Peptide gamma"
FT /id="PRO_0000039195"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..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"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 69..318
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 90..105
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 161..177
FT /evidence="ECO:0007829|PDB:4FTB"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:4FTB"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 309..323
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:4FTB"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4FTB"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:4FTB"
SQ SEQUENCE 407 AA; 43710 MW; 5A66E01BAD2FEB0B CRC64;
MVNNNRPRRQ RAQRVVVTTT QTAPVPQQNV PRNGRRRRNR TRRNRRRVRG MNMAALTRLS
QPGLAFLKCA FAPPDFNTDP GKGIPDRFEG KVVSRKDVLN QSISFTAGQD TFILIAPTPG
VAYWSASVPA GTFPTSATTF NPVNYPGFTS MFGTTSTSRS DQVSSFRYAS MNVGIYPTSN
LMQFAGSITV WKCPVKLSTV QFPVATDPAT SSLVHTLVGL DGVLAVGPDN FSESFIKGVF
SQSACNEPDF EFNDILEGIQ TLPPANVSLG STGQPFTMDS GAEATSGVVG WGNMDTIVIR
VSAPEGAVNS AILKAWSCIE YRPNPNAMLY QFGHDSPPLD EVALQEYRTV ARSLPVAVIA
AQNASMWERV KSIIKSSLAA ASNIPGPIGV AASGISGLSA LFEGFGF
