ID   CAPSD_CARMS             Reviewed;         348 AA.
AC   Q9Q6X7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 55.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE   AltName: Full=p38;
GN   ORFNames=ORF4;
OS   Carnation mottle virus (isolate China/Shanghai) (CarMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Alphacarmovirus.
OX   NCBI_TaxID=652111;
OH   NCBI_TaxID=278075; Dianthus barbatus.
OH   NCBI_TaxID=3570; Dianthus caryophyllus (Carnation) (Clove pink).
OH   NCBI_TaxID=118431; Dianthus chinensis.
OH   NCBI_TaxID=288950; Dianthus superbus.
OH   NCBI_TaxID=3572; Saponaria officinalis (Common soapwort) (Lychnis saponaria).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Zhang A.P., Yue Y., Ye R., Zhu H.Q., Xu L., Yu S.Q.;
RT   "Infectivity of full-length cDNA of carnation mottle virus.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC       with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180
CC       capsid proteins. Also acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing (PTGS), a
CC       mechanism of plant viral defense that limits the accumulation of viral
CC       RNAs (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds Ca(2+). Ca(2+) probably promotes virus assembly and
CC       stabilizes the virus particle. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Homomultimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF192772; AAF15526.1; -; Genomic_RNA.
DR   SMR; Q9Q6X7; -.
DR   Proteomes; UP000006709; 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; IPR013669; Coat_prot_C_Carmovir.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF08462; Carmo_coat_C; 1.
DR   Pfam; PF00729; Viral_coat; 1.
DR   PRINTS; PR00233; ICOSAHEDRAL.
DR   PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE   3: Inferred from homology;
KW   Calcium; Capsid protein; Reference proteome; RNA-binding;
KW   T=3 icosahedral capsid protein; Virion.
FT   CHAIN           1..348
FT                   /note="Capsid protein"
FT                   /id="PRO_0000398301"
FT   REGION          58..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..239
FT                   /note="S domain, virion shell"
FT   REGION          240..348
FT                   /note="P domain, projecting"
FT   COMPBIAS        64..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  37738 MW;  CF9860CD9D9A7815 CRC64;
     MENKGEKIAM NPTVQTLAQK GDKLAVKLVT RGWASLSTNQ KRRAEMLAGY TPAILAFTPR
     RPRMTNSPPR TSRNSPGQAG KSMTMSKTEL LCTVKGTTGV IPSFEDWVVS PRNVAVFPQL
     SLLATNFNKY RITALTVKYS PACSFETNGR VALGFNDDAS DTPPTTKVGF YDLGKHVETA
     AQTAKDLVIP VDGKTRFIRD SASDDAKLVD FGRLVLSTYG FDKADTVVGE LFIQYTIVLS
     DPTKTAKISQ ASNDKVSDGP TYVVPSVNGN ELQLRVVAAG KWCIIVRGTV EGGFTKPTLI
     GPGISGDVDY ESARPIAICE LVTQMEGQML KITKTSAEQP LKVVVYRM