ID   CAPSD_CNV               Reviewed;         380 AA.
AC   P15183;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE   AltName: Full=p41;
GN   ORFNames=ORF2;
OS   Cucumber necrosis virus (CNV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Tombusvirus;
OC   Tombusvirus cucumis.
OX   NCBI_TaxID=12143;
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2705296; DOI=10.1016/0042-6822(89)90150-5;
RA   Rochon D.M., Tremaine J.H.;
RT   "Complete nucleotide sequence of the cucumber necrosis virus genome.";
RL   Virology 169:251-259(1989).
RN   [2]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=20483445; DOI=10.1016/j.virol.2010.03.045;
RA   Reade R., Kakani K., Rochon D.;
RT   "A highly basic KGKKGK sequence in the RNA-binding domain of the Cucumber
RT   necrosis virus coat protein is associated with encapsidation of full-length
RT   CNV RNA during infection.";
RL   Virology 403:181-188(2010).
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. {ECO:0000269|PubMed:20483445}.
CC   -!- SUBUNIT: Homomultimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC       {ECO:0000305}.
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DR   EMBL; M25270; AAA42904.1; -; Genomic_RNA.
DR   PIR; JA0131; VCVGCN.
DR   RefSeq; NP_040955.1; NC_001469.1.
DR   PDB; 4LLF; X-ray; 2.89 A; A/B/D/E/F/G/H/I/J/K/L/M/N/O/P=1-380.
DR   PDBsum; 4LLF; -.
DR   SMR; P15183; -.
DR   GeneID; 1493950; -.
DR   KEGG; vg:1493950; -.
DR   OrthoDB; 10131at10239; -.
DR   Proteomes; UP000008565; 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   Gene3D; 2.60.40.4030; -; 1.
DR   InterPro; IPR000937; Capsid_prot_S-dom_vir.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00729; Viral_coat; 1.
DR   PRINTS; PR00233; ICOSAHEDRAL.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR   PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; RNA-binding; T=3 icosahedral capsid protein;
KW   Virion.
FT   CHAIN           1..380
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222861"
FT   REGION          1..92
FT                   /note="R domain, interaction with RNA"
FT   REGION          48..53
FT                   /note="Involved in encapsidation"
FT                   /evidence="ECO:0000305"
FT   REGION          93..254
FT                   /note="S domain, virion shell"
FT   REGION          255..380
FT                   /note="P domain, projecting"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          94..107
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   HELIX           138..141
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          144..158
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          167..175
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          191..196
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          230..237
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          241..257
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          264..269
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          302..310
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          319..324
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          327..334
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          339..347
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          352..355
FT                   /evidence="ECO:0007829|PDB:4LLF"
FT   STRAND          364..370
FT                   /evidence="ECO:0007829|PDB:4LLF"
SQ   SEQUENCE   380 AA;  40878 MW;  793CB6B05CEC6669 CRC64;
     MALVSRNNNM RTLAKLAAPL ATAGTRTIVD NKEAIWNGVK WIWGKLPKGK KGKNGNGALI
     AHPQAFPGAI AAPISYAYAV KGRKPRFQTA KGSVRITHRE YVSVLSGTNG EFLRNNGTGP
     NNDFSINPLN PFLFPWLVNI AANFDQYKFN SLRFEYVPLV NTTTNGRVAL YFDKDSEDPG
     PDDRAALANY AHLSEISPWA ITKLTVPTDN VKRFISDTSS GDPKLINLGQ FGWVAYSGPT
     AELGDIFVEY TVDLFEAQPT SPLLESLFRE SASSVQTRMG LPYFSLEVAS ATDLVWQARV
     PGTYVVTIIF NSTVGGLTPS ISGGGTINSS FSVSTAGSSA YVANITIRVN ANLSLSGLTG
     ATNAQLFAVR AITENAVQVV
//