ID   CAPSD_CMVKI             Reviewed;         218 AA.
AC   Q06934;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF3b;
OS   Cucumber mosaic virus (strain Kin) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=36400;
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=8460476; DOI=10.1006/viro.1993.1165;
RA   Boccard F., Baulcombe D.;
RT   "Mutational analysis of cis-acting sequences and gene function in RNA3 of
RT   cucumber mosaic virus.";
RL   Virology 193:563-578(1993).
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).
RN   [3]
RP   FUNCTION, AND DOMAIN ARG-RICH MOTIF.
RX   PubMed=9721241; DOI=10.1006/viro.1998.9257;
RA   Schmitz I., Rao A.L.;
RT   "Deletions in the conserved amino-terminal basic arm of cucumber mosaic
RT   virus coat protein disrupt virion assembly but do not abolish infectivity
RT   and cell-to-cell movement.";
RL   Virology 248:323-331(1998).
CC   -!- FUNCTION: Capsid protein. Probably binds RNA and plays a role in
CC       packaging (By similarity). {ECO:0000250, ECO:0000269|PubMed:9721241}.
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:0000269|PubMed:9721241}.
CC   -!- SIMILARITY: Belongs to the cucumovirus capsid 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; Z12818; CAA78279.1; -; Genomic_RNA.
DR   PIR; B46111; B46111.
DR   SMR; Q06934; -.
DR   iPTMnet; Q06934; -.
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_0000083209"
FT   REGION          1..30
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;  24202 MW;  E39EFD53FDD8285B CRC64;
     MDKSGSPNAS RTSRRRRPRR GSRSASGADA GLRALTQQML KLNKTLAIGR PTLNHPTFVG
     SESCKPGYTF TSITLKPPEI EKGSYFGRRL SLPDSVTDYD KKLVSRIQIR INPLPKFDST
     VWVTVRKVPS SSDLSVAAIS AMFGDGNSPV LVYQYAASGV QANNKLLYDL SEMRADIGDM
     RKYAVLVYSK DDNLEKDEIV LHVDVEHQRI PISRMLPT