CAPSD_AMCV
ID CAPSD_AMCV Reviewed; 388 AA.
AC P14836;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE AltName: Full=p41;
GN ORFNames=ORF2;
OS Artichoke mottled crinkle virus (AMCV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Procedovirinae; Tombusvirus.
OX NCBI_TaxID=12142;
OH NCBI_TaxID=59895; Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Bari-Dr. Gallitelli isolate;
RX PubMed=2320427; DOI=10.1093/nar/18.5.1300;
RA Grieco F., Gallitelli D.;
RT "Nucleotide sequence of the 3'-terminal region of artichoke mottled crinkle
RT tombusvirus RNA.";
RL Nucleic Acids Res. 18:1300-1300(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Bari-Dr. Gallitelli isolate;
RX PubMed=2491684; DOI=10.1007/bf00016023;
RA Tavazza M., Lucioli A., Ancora G., Benvenuto E.;
RT "cDNA cloning of artichoke mottled crinkle virus RNA and localization and
RT sequencing of the coat protein gene.";
RL Plant Mol. Biol. 13:685-692(1989).
RN [3]
RP SEQUENCE REVISION.
RA Tavazza M.;
RL Submitted (OCT-1991) 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.
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; X51456; CAA35821.1; -; Genomic_RNA.
DR EMBL; X16060; CAA34196.1; -; Genomic_RNA.
DR EMBL; X62493; CAA44357.1; -; Genomic_RNA.
DR PIR; S08428; VCVGAC.
DR PIR; S24926; S24926.
DR RefSeq; NP_039810.1; NC_001339.1.
DR SMR; P14836; -.
DR GeneID; 1493940; -.
DR KEGG; vg:1493940; -.
DR Proteomes; UP000202336; 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; IPR029053; Viral_coat.
DR Pfam; PF00729; Viral_coat; 1.
DR PRINTS; PR00233; ICOSAHEDRAL.
DR PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE 3: Inferred from homology;
KW Capsid protein; RNA-binding; T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..388
FT /note="Capsid protein"
FT /id="PRO_0000222859"
FT REGION 1..102
FT /note="R domain, interaction with RNA"
FT REGION 56..61
FT /note="Involved in encapsidation"
FT /evidence="ECO:0000250"
FT REGION 103..263
FT /note="S domain, virion shell"
FT REGION 264..388
FT /note="P domain, projecting"
FT CONFLICT 17
FT /note="T -> M (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> R (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> I (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> I (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="FR -> IC (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="V -> L (in Ref. 1; CAA35821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 41164 MW; D8636A99AEC60BC0 CRC64;
MAMVKRNNNT GLIPVSTKQL MALGAAAGAS ALQGFVRNNG AAIVGKVVDV GQKVYKAVKK
RGGKKQQQIK HVGGTGGAIM APVAVTRQLT GSKPKFTGKT SGSVTVTHRE YLSQVNMSTG
FQVNGGIVGN LLQLNPLNGT LFSWLPAIAS NFDQYSFNSV LLHYVPLCAT TEVGRVAMYF
DKDSEDPEPA DRVELANYSV LAETAPWAER ALWVPTDRIK RFCDDSSTLD HKLIDLGQLG
VATYGGAGTN AVGDIFISYS VTLYFPQPTN TLLSTRRLDL AGTPVTASGP GYILLTRTPT
VLTMTFRATG TFVISGAYRC LTSTVLGLTG GVNVNSITVV DNVGTSSSFF INCTVSNLPS
VITFTTTGIT SATIQCNRAT RQNDVSLI