CAPSD_CARMV
ID CAPSD_CARMV Reviewed; 348 AA.
AC P04383;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE AltName: Full=p38;
GN ORFNames=ORF4;
OS Carnation mottle virus (CarMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Procedovirinae; Alphacarmovirus.
OX NCBI_TaxID=11986;
OH NCBI_TaxID=3681; Begonia.
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=3750; Malus domestica (Apple) (Pyrus malus).
OH NCBI_TaxID=3572; Saponaria officinalis (Common soapwort) (Lychnis saponaria).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3840587; DOI=10.1093/nar/13.18.6663;
RA Guilley H., Carrington J.C., Balazs E., Jonard G., Richards K.,
RA Morris T.J.;
RT "Nucleotide sequence and genome organization of carnation mottle virus
RT RNA.";
RL Nucleic Acids Res. 13:6663-6677(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=8307192; DOI=10.1016/0014-5793(94)80281-5;
RA Morgunova E.Y., Dauter Z., Stuart D.I., Stel'Mashchuk V.Y., Mikhailov A.M.,
RA Wilson K.S., Vainshtein B.K.;
RT "The atomic structure of Carnation mottle virus capsid protein.";
RL FEBS Lett. 338:267-271(1994).
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 stabilize 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}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1opo";
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DR EMBL; X02986; CAA26728.1; -; Genomic_RNA.
DR PIR; A04209; VCVECV.
DR RefSeq; YP_009032648.1; NC_001265.2.
DR PDB; 1OPO; X-ray; 3.20 A; A/B/C=1-348.
DR PDBsum; 1OPO; -.
DR SMR; P04383; -.
DR GeneID; 19493256; -.
DR KEGG; vg:19493256; -.
DR EvolutionaryTrace; P04383; -.
DR Proteomes; UP000201784; 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 DisProt; DP02071; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000222860"
FT REGION 59..86
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 67..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1OPO"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1OPO"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 127..141
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1OPO"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1OPO"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 227..242
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1OPO"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1OPO"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:1OPO"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:1OPO"
SQ SEQUENCE 348 AA; 37787 MW; E9EEA336C45B0D39 CRC64;
MENKGEKIAM NPTVQTLAQK GDKLAVKLVT RGWASLSTNQ KRRAEMLAGY TPAILAFTPR
RPRMTNPPPR TSRNSPGQAG KSMTMSKTEL LSTVKGTTGV IPSFEDWVVS PRNVAVFPQL
SLLATNFNKY RITALTVKYS PACSFETNGR VALGFNDDAS DTPPTTKVGF YDLGKHVETA
AQTAKDLVIP VDGKTRFIRD SASDDAKLVD FGRIVLSTYG FDKADTVVGE LFIQYTIVLS
DPTKTAKISQ ASNDKVSDGP TYVVPSVNGN ELQLRVVAAG KWCIIVRGTV EGGFTKPTLI
GPGISGDVDY ESARPIAVCE LVTQMEGQIL KITKTSAEQP LQWVVYRM
