ID   CAPSD_RCNMV             Reviewed;         339 AA.
AC   P22955;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   02-JUN-2021, entry version 77.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF2;
OS   Red clover necrotic mosaic virus (RCNMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Regressovirinae; Dianthovirus.
OX   NCBI_TaxID=12267;
OH   NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH   NCBI_TaxID=47083; Melilotus officinalis (Yellow sweet clover) (Trifolium officinale).
OH   NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH   NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Australian;
RX   PubMed=2763465; DOI=10.1016/0042-6822(89)90624-7;
RA   Xiong Z., Lommel S.A.;
RT   "The complete nucleotide sequence and genome organization of red clover
RT   necrotic mosaic virus RNA-1.";
RL   Virology 171:543-554(1989).
RN   [2]
RP   FUNCTION, DOMAIN, MUTAGENESIS OF LYS-4; LYS-7 AND LYS-8, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=22292426; DOI=10.1111/j.1364-3703.2011.00784.x;
RA   Park S.H., Sit T.L., Kim K.H., Lommel S.A.;
RT   "The Red clover necrotic mosaic virus capsid protein N-terminal lysine-rich
RT   motif is a determinant of symptomatology and virion accumulation.";
RL   Mol. Plant Pathol. 13:744-754(2012).
RN   [3]
RP   FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=23747688; DOI=10.1016/j.virusres.2013.05.014;
RA   Park S.H., Sit T.L., Kim K.H., Lommel S.A.;
RT   "The red clover necrotic mosaic virus capsid protein N-terminal amino acids
RT   possess specific RNA binding activity and are required for stable virion
RT   assembly.";
RL   Virus Res. 176:107-118(2013).
CC   -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC       with a T=3 symmetry, about 31-34 nm in diameter, and consisting of 180
CC       capsid proteins. Plays an essential role in virion formation by
CC       interacting, via its N-terminal region, with the bipartite viral RNA
CC       genome and specifically with the 3' terminus of RNA-1 and the TA
CC       element on RNA-2. Participates also in symptom development, viral RNA
CC       accumulation and systemic movement within the host.
CC       {ECO:0000269|PubMed:22292426, ECO:0000269|PubMed:23747688}.
CC   -!- SUBUNIT: Homomultimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:22292426,
CC       ECO:0000269|PubMed:23747688}.
CC   -!- DOMAIN: The N-terminal R domain is rich in basic residues and is
CC       essential for RNA-binding and virion assembly functions.
CC       {ECO:0000269|PubMed:22292426}.
CC   -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC       {ECO:0000305}.
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DR   EMBL; J04357; AAB02542.1; -; Genomic_RNA.
DR   PIR; C43684; C43684.
DR   RefSeq; NP_620526.1; NC_003756.1.
DR   PDB; 6MRM; EM; 2.90 A; A/B/C=1-339.
DR   PDBsum; 6MRM; -.
DR   SMR; P22955; -.
DR   GeneID; 24271523; -.
DR   KEGG; vg:24271523; -.
DR   Proteomes; UP000008651; Genome.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR000937; Capsid_prot_S-dom_vir.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00729; Viral_coat; 1.
DR   PRINTS; PR00233; ICOSAHEDRAL.
DR   PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Reference proteome; RNA-binding;
KW   T=3 icosahedral capsid protein; Virion.
FT   CHAIN           1..339
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222865"
FT   REGION          1..46
FT                   /note="R domain, interaction with RNA"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..207
FT                   /note="S domain, virion shell"
FT   REGION          208..339
FT                   /note="P domain, projecting"
FT   MUTAGEN         4
FT                   /note="K->A: Strongly impairs the systemic spread of viral
FT                   genomes."
FT                   /evidence="ECO:0000269|PubMed:22292426"
FT   MUTAGEN         7
FT                   /note="K->A: Strongly impairs the systemic spread of viral
FT                   genomes; in association with A-8."
FT                   /evidence="ECO:0000269|PubMed:22292426"
FT   MUTAGEN         8
FT                   /note="K->A: Strongly impairs the systemic spread of viral
FT                   genomes; in association with A-7."
FT                   /evidence="ECO:0000269|PubMed:22292426"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   HELIX           89..93
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          96..105
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   TURN            137..141
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          142..149
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          194..210
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          241..244
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          258..266
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          291..302
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:6MRM"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:6MRM"
SQ   SEQUENCE   339 AA;  36583 MW;  985DC663E6431AF0 CRC64;
     MSSKAPKKSK QRSQPRNRTP NTSVKTVAIP FAKTQIIKTV NPPPKPARGI LHTQLVMSVV
     GSVQMRTNNG KSNQRFRLNP SNPALFPTLA YEAANYDMYR LKKLTLRYVP LVTVQNSGRV
     AMIWDPDSQD SAPQSRQEIS AYSRSVSTAV YEKCSLTIPA DNQWRFVADN TTVDRKLVDF
     GQLLFVTHSG SDGIETGDIF LDCEVEFKGP QPTASIVQKT VIDLGGTLTS FEGPSYLMPP
     DAFITSSSFG LFVDVAGTYL LTLVVTCSTT GSVTVGGNST LVGDGRAAYG SSNYIASIVF
     TSSGVLSTTP SVQFSGSSGV SRVQMNICRC KQGNTFILG