CAPSD_BMV
ID CAPSD_BMV Reviewed; 189 AA.
AC P03602;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
GN ORFNames=ORF3b;
OS Brome mosaic virus (BMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Bromovirus.
OX NCBI_TaxID=12302;
OH NCBI_TaxID=15371; Bromus inermis (Smooth brome grass) (Bromopsis inermis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7338913; DOI=10.1016/0022-2836(81)90524-6;
RA Ahlquist P., Luckow V., Kaesberg P.;
RT "Complete nucleotide sequence of brome mosaic virus RNA3.";
RL J. Mol. Biol. 153:23-38(1981).
RN [2]
RP FUNCTION, AND DOMAIN ARG-RICH MOTIF.
RX PubMed=11017800; DOI=10.1006/viro.2000.0513;
RA Choi Y.G., Rao A.L.;
RT "Molecular studies on bromovirus capsid protein. VII. Selective packaging
RT on BMV RNA4 by specific N-terminal arginine residuals.";
RL Virology 275:207-217(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RX PubMed=11916381; DOI=10.1006/jmbi.2001.5389;
RA Lucas R.W., Larson S.B., McPherson A.;
RT "The crystallographic structure of brome mosaic virus.";
RL J. Mol. Biol. 317:95-108(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-189.
RX PubMed=15713465; DOI=10.1016/j.jmb.2004.12.015;
RA Larson S.B., Lucas R.W., McPherson A.;
RT "Crystallographic structure of the T=1 particle of brome mosaic virus.";
RL J. Mol. Biol. 346:815-831(2005).
CC -!- FUNCTION: Capsid protein. Binds specifically to the subgenomic RNA4 to
CC ensure selective packaging. {ECO:0000269|PubMed:11017800}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: The N-terminal arginine-rich region binds selectively to
CC subgenomic RNA4. {ECO:0000269|PubMed:11017800}.
CC -!- SIMILARITY: Belongs to the bromovirus capsid protein family.
CC {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=1yc6";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1js9";
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DR EMBL; J02042; AAA46334.1; -; Genomic_RNA.
DR PIR; A04213; VCBVM.
DR RefSeq; NP_041199.1; NC_002028.2.
DR PDB; 1JS9; X-ray; 3.40 A; A/B/C=1-189.
DR PDB; 1YC6; X-ray; 2.90 A; 1/2/3/4/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=36-189.
DR PDB; 3J7L; EM; 3.80 A; A/B/C=1-189.
DR PDB; 3J7M; EM; 3.80 A; A/B/C=1-189.
DR PDB; 3J7N; EM; 3.80 A; A/B/C=1-189.
DR PDB; 6VOC; EM; 3.10 A; A/B/C=1-189.
DR PDBsum; 1JS9; -.
DR PDBsum; 1YC6; -.
DR PDBsum; 3J7L; -.
DR PDBsum; 3J7M; -.
DR PDBsum; 3J7N; -.
DR PDBsum; 6VOC; -.
DR SMR; P03602; -.
DR GeneID; 962148; -.
DR KEGG; vg:962148; -.
DR EvolutionaryTrace; P03602; -.
DR Proteomes; UP000001649; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR002009; Bromo_CP.
DR Pfam; PF01318; Bromo_coat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; T=3 icosahedral capsid protein; Viral nucleoprotein; Virion.
FT CHAIN 1..189
FT /note="Capsid protein"
FT /id="PRO_0000083194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1YC6"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1YC6"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1YC6"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1YC6"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1YC6"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1YC6"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:1YC6"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:1YC6"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1JS9"
SQ SEQUENCE 189 AA; 20385 MW; D0FDB05C608C66E5 CRC64;
MSTSGTGKMT RAQRRAAARR NRWTARVQPV IVEPLAAGQG KAIKAIAGYS ISKWEASSDA
ITAKATNAMS ITLPHELSSE KNKELKVGRV LLWLGLLPSV AGRIKACVAE KQAQAEAAFQ
VALAVADSSK EVVAAMYTDA FRGATLGDLL NLQIYLYASE AVPAKAVVVH LEVEHVRPTF
DDFFTPVYR
