CAPSD_CFMVN
ID CAPSD_CFMVN Reviewed; 254 AA.
AC Q66012; Q0PW23;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 63.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
DE AltName: Full=Protein P4;
GN ORFNames=ORF3;
OS Cocksfoot mottle virus (isolate Dactylis glomerata/Norway/CfMV-NO/1995)
OS (CfMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Sobemovirus.
OX NCBI_TaxID=1005059;
OH NCBI_TaxID=4509; Dactylis glomerata (Orchard grass) (Cock's-foot grass).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 3-19.
RX PubMed=7595389; DOI=10.1099/0022-1317-76-11-2817;
RA Maekinen K., Tamm T., Naess V., Truve E., Puurand U., Munthe T., Saarma M.;
RT "Characterization of cocksfoot mottle sobemovirus genomic RNA and sequence
RT comparison with related viruses.";
RL J. Gen. Virol. 76:2817-2825(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16732485; DOI=10.1007/s11262-005-6917-x;
RA Meier M., Paves H., Olspert A., Tamm T., Truve E.;
RT "P1 protein of Cocksfoot mottle virus is indispensable for the systemic
RT spread of the virus.";
RL Virus Genes 32:321-326(2006).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 30 nm in diameter, and consisting of 180
CC capsid proteins. Each icosahedral unit contains three protein subunits
CC (Potential). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC {ECO:0000305}.
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DR EMBL; Z48630; CAA88562.1; -; Genomic_RNA.
DR EMBL; DQ680848; ABG73620.1; -; Genomic_RNA.
DR RefSeq; NP_941377.1; NC_002618.2.
DR SMR; Q66012; -.
DR GeneID; 2654594; -.
DR KEGG; vg:2654594; -.
DR Proteomes; UP000001461; Genome.
DR Proteomes; UP000008994; 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 PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Reference proteome; RNA-binding;
KW T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..254
FT /note="Capsid protein"
FT /id="PRO_0000409863"
FT REGION 1..61
FT /note="R domain, interaction with RNA"
FT /evidence="ECO:0000250"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..245
FT /note="S domain, virion shell"
FT /evidence="ECO:0000250"
FT REGION 246..254
FT /note="P domain, projecting"
FT /evidence="ECO:0000250"
FT CONFLICT 174
FT /note="V -> M (in Ref. 2; ABG73620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27610 MW; 871321630970DC9C CRC64;
MMVRKGAATK APQQPKPKAQ QQPGGRRRRR GRSMEPVSRP LNPPAAVGST LKAGRGRTAG
VSDWFDTGMI TSYLGGFQRT AGTTDSQVFI VSPAALDRVG TIAKAYALWR PKHWEIVYLP
RCSTQTDGSI EMGFLLDYAD SVPTNTRTMA SSTSFTTSNV WGGGDGSSLL HTSVKSMGNA
VTSALPCDEF SNKWFKLSWS TPEESENAHL TDTYVPARFV VRSDFPVVTA DQPGHLWLRS
RILLKGSVSP STNL