ID   CAPSD_PSVJ              Reviewed;         217 AA.
AC   P22116;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF3b;
OS   Peanut stunt virus (strain J) (PSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12314;
OH   NCBI_TaxID=4045; Apium graveolens (Celery).
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=53860; Coronilla.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH   NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=3914; Phaseolus angularis (Azuki bean) (Vigna angularis).
OH   NCBI_TaxID=47097; Tephrosia.
OH   NCBI_TaxID=3898; Trifolium.
OH   NCBI_TaxID=3904; Vicia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1926787; DOI=10.1016/0042-6822(91)90800-q;
RA   Karasawa A., Nakaho K., Kakutani T., Minobe Y., Ehara Y.;
RT   "Nucleotide sequence of RNA 3 of peanut stunt cucumovirus.";
RL   Virology 185:464-467(1991).
CC   -!- FUNCTION: Capsid protein. Probably binds RNA and plays a role in
CC       packaging (By similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the cucumovirus capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00668; BAA00572.1; -; Genomic_RNA.
DR   PIR; B40786; VCVXPS.
DR   SMR; P22116; -.
DR   PRIDE; P22116; -.
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   Gene3D; 2.60.120.530; -; 1.
DR   InterPro; IPR000247; Cucumovirus_coat.
DR   InterPro; IPR023800; Cucumovirus_coat_A.
DR   InterPro; IPR037137; Cucumovirus_coat_Asu_sf.
DR   Pfam; PF00760; Cucumo_coat; 1.
DR   PRINTS; PR00222; CUCUMOCOAT.
PE   3: Inferred from homology;
KW   Acetylation; Capsid protein; Disulfide bond; Ribonucleoprotein;
KW   RNA-binding; T=3 icosahedral capsid protein; Viral nucleoprotein; Virion.
FT   CHAIN           1..217
FT                   /note="Capsid protein"
FT                   /id="PRO_0000083223"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; by host"
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..105
FT                   /evidence="ECO:0000250|UniProtKB:P23627"
SQ   SEQUENCE   217 AA;  24180 MW;  627ECCC42CD72A1B CRC64;
     MASKGSGNGS RRPRRGRRSF PIKEDAHARE LRAVTAQLNR LVALTAARMP TLDHPTFVSS
     RKCAKGYTYT SLDVRPTKTE KGHSFGQRLN LPVPVSEFPK KKVSCVQLRL NPSPTFDSTV
     WVTLRKLPLG YSLASESVFK LFTDGLSAVL MYQHVPNGIQ RDNKIIYDLS PVGTEIGDMS
     EYAIIVYSKD DTLEDDEILI HVDVEHQRIP SATALPV