CAPSD_CCMV
ID CAPSD_CCMV Reviewed; 190 AA.
AC P03601;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
GN ORFNames=ORF3b;
OS Cowpea chlorotic mottle virus (CCMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Bromovirus.
OX NCBI_TaxID=12303;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2773323; DOI=10.1016/0042-6822(89)90134-7;
RA Allison R.F., Janda M., Ahlquist P.;
RT "Sequence of cowpea chlorotic mottle virus RNAs 2 and 3 and evidence of a
RT recombination event during bromovirus evolution.";
RL Virology 172:321-330(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6895941; DOI=10.1093/nar/10.2.703;
RA Dasgupta R., Kaesberg P.;
RT "Complete nucleotide sequences of the coat protein messenger RNAs of brome
RT mosaic virus and cowpea chlorotic mottle virus.";
RL Nucleic Acids Res. 10:703-713(1982).
RN [3]
RP FUNCTION, AND DOMAIN ARG-RICH MOTIF.
RX PubMed=15731222; DOI=10.1128/jvi.79.6.3277-3288.2005;
RA Annamalai P., Apte S., Wilkens S., Rao A.L.;
RT "Deletion of highly conserved arginine-rich RNA binding motif in cowpea
RT chlorotic mottle virus capsid protein results in virion structural
RT alterations and RNA packaging constraints.";
RL J. Virol. 79:3277-3288(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=7743132; DOI=10.1016/s0969-2126(01)00135-6;
RA Speir J.A., Munshi S., Wang G., Baker T.S., Johnson J.E.;
RT "Structures of the native and swollen forms of cowpea chlorotic mottle
RT virus determined by X-ray crystallography and cryo-electron microscopy.";
RL Structure 3:63-78(1995).
RN [5]
RP STRUCTURE BY NMR OF 1-26, AND ACETYLATION AT SER-2.
RX PubMed=1935944; DOI=10.1111/j.1432-1033.1991.tb16307.x;
RA van der Graaf M., Hemminga M.A.;
RT "Conformational studies on a peptide fragment representing the RNA-binding
RT N-terminus of a viral coat protein using circular dichroism and NMR
RT spectroscopy.";
RL Eur. J. Biochem. 201:489-494(1991).
RN [6]
RP STRUCTURE BY NMR OF 1-26.
RX PubMed=1904274; DOI=10.1021/bi00237a013;
RA van der Graaf M., van Mierlo C.P.M., Hemminga M.A.;
RT "Solution conformation of a peptide fragment representing a proposed RNA-
RT binding site of a viral coat protein studied by two-dimensional NMR.";
RL Biochemistry 30:5722-5727(1991).
RN [7]
RP STRUCTURE BY NMR OF 1-34.
RX PubMed=1908015; DOI=10.1016/0022-2836(91)90111-i;
RA van der Graaf M., Kroon G.J.A., Hemminga M.A.;
RT "Conformation and mobility of the RNA-binding N-terminal part of the intact
RT coat protein of cowpea chlorotic mottle virus. A two-dimensional proton
RT nuclear magnetic resonance study.";
RL J. Mol. Biol. 220:701-709(1991).
CC -!- FUNCTION: Capsid protein. Probably binds RNA and plays a role in
CC packaging. {ECO:0000269|PubMed:15731222}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: The N-terminal arginine-rich stretch does not seem to be the
CC major RNA-binding region that allows formation of an infectious
CC ribonucleoprotein complex. {ECO:0000269|PubMed:15731222}.
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=rcmv";
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DR EMBL; M28818; AAA46373.1; -; Genomic_RNA.
DR EMBL; J02052; AAA46370.1; -; Genomic_RNA.
DR PIR; A04212; VCBVC.
DR RefSeq; NP_613277.1; NC_003542.1.
DR PDB; 1CWP; X-ray; 3.20 A; A/B/C=1-190.
DR PDB; 1ZA7; X-ray; 2.70 A; A/B/C=26-190.
DR PDBsum; 1CWP; -.
DR PDBsum; 1ZA7; -.
DR BMRB; P03601; -.
DR SMR; P03601; -.
DR iPTMnet; P03601; -.
DR GeneID; 962152; -.
DR KEGG; vg:962152; -.
DR EvolutionaryTrace; P03601; -.
DR Proteomes; UP000008445; Genome.
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; Acetylation; Capsid protein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; T=3 icosahedral capsid protein;
KW Viral nucleoprotein; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..190
FT /note="Capsid protein"
FT /id="PRO_0000083195"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine; by host"
FT /evidence="ECO:0000269|PubMed:1935944"
FT CONFLICT 151
FT /note="T -> A (in Ref. 2; AAA46370)"
FT /evidence="ECO:0000305"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1ZA7"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1ZA7"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:1ZA7"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1ZA7"
SQ SEQUENCE 190 AA; 20343 MW; 36BD1DA882D27EAD CRC64;
MSTVGTGKLT RAQRRAAARK NKRNTRVVQP VIVEPIASGQ GKAIKAWTGY SVSKWTASCA
AAEAKVTSAI TISLPNELSS ERNKQLKVGR VLLWLGLLPS VSGTVKSCVT ETQTTAAASF
QVALAVADNS KDVVAAMYPE AFKGITLEQL TADLTIYLYS SAALTEGDVI VHLEVEHVRP
TFDDSFTPVY
