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 24-JAN-2024, entry version 80. 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; OC Dianthovirus trifolii. 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}. 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; 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 EMDB; EMD-9205; -. DR SMR; P22955; -. DR GeneID; 24271523; -. DR KEGG; vg:24271523; -. DR OrthoDB; 10131at10239; -. 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 Gene3D; 2.60.40.4030; -; 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 SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1. 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 //