ID   CAPSD_CMVFC             Reviewed;         218 AA.
AC   Q00259;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-JUN-2021, entry version 74.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF3b;
OS   Cucumber mosaic virus (strain FC) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=31717;
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1919534; DOI=10.1099/0022-1317-72-10-2587;
RA   Shintaku M.;
RT   "Coat protein gene sequences of two cucumber mosaic virus strains reveal a
RT   single amino acid change correlating with chlorosis induction.";
RL   J. Gen. Virol. 72:2587-2589(1991).
RN   [2]
RP   ACETYLATION AT MET-1.
RX   PubMed=6754709; DOI=10.1093/oxfordjournals.jbchem.a133971;
RA   Tsunasawa S., Narita K.;
RT   "Micro-identification of amino-terminal acetylamino acids in proteins.";
RL   J. Biochem. 92:607-613(1982).
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; D10544; BAA01403.1; -; Genomic_RNA.
DR   PIR; JQ1253; JQ1253.
DR   SMR; Q00259; -.
DR   iPTMnet; Q00259; -.
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   1: Evidence at protein level;
KW   Acetylation; Capsid protein; Ribonucleoprotein; RNA-binding;
KW   T=3 icosahedral capsid protein; Viral nucleoprotein; Virion.
FT   CHAIN           1..218
FT                   /note="Capsid protein"
FT                   /id="PRO_0000083203"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; by host"
FT                   /evidence="ECO:0000269|PubMed:6754709"
SQ   SEQUENCE   218 AA;  24131 MW;  C4B7CFB12F2A7CAB CRC64;
     MDKSESTSAG RNRRRRPRRG SRSAPSSADA NFRVLSQQLS RLNKTLAAGR PTINHPTFVG
     SERCRPGYTF TSITLKPPKI DRGSYYGKRL LLPDSVTEYD KKLVSRIQIR VNPLPKFDST
     VWVTVRKVSA SSDLSVAAIS AMFADGASPV LVYQYAASGV QANNKLLYDL SAMRADIGDM
     RKYAVLVYSK DDALETDELV LHVDIEHQRI PTSGVLPV