ID CAPSD_STNV1 Reviewed; 196 AA. AC P03606; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 08-NOV-2023, entry version 115. DE RecName: Full=Capsid protein {ECO:0000305}; DE AltName: Full=Coat protein {ECO:0000305}; OS Satellite tobacco necrosis virus 1. OC Viruses; Riboviria; Albetovirus; Tobacco albetovirus 1. OX NCBI_TaxID=12445; OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean). OH NCBI_TaxID=13306; Tulipa gesneriana (Garden tulip). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=6260960; DOI=10.1016/0022-2836(80)90190-4; RA Ysebaert M., van Emmelo J., Fiers W.; RT "Total nucleotide sequence of a nearly full-size DNA copy of satellite RT tobacco necrosis virus RNA."; RL J. Mol. Biol. 143:273-287(1980). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND FUNCTION. RX PubMed=6481804; DOI=10.1016/0022-2836(84)90047-0; RA Jones T.A., Liljas L.; RT "Structure of satellite tobacco necrosis virus after crystallographic RT refinement at 2.5-A resolution."; RL J. Mol. Biol. 177:735-767(1984). RN [3] {ECO:0007744|PDB:3S4G, ECO:0007744|PDB:4V4M} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION, RP AND COFACTOR. RX PubMed=21839089; DOI=10.1016/j.jmb.2011.07.062; RA Lane S.W., Dennis C.A., Lane C.L., Trinh C.H., Rizkallah P.J., RA Stockley P.G., Phillips S.E.; RT "Construction and crystal structure of recombinant STNV capsids."; RL J. Mol. Biol. 413:41-50(2011). RN [4] {ECO:0007744|PDB:4BCU} RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION, RP AND RNA-BINDING. RX PubMed=23318955; DOI=10.1016/j.jmb.2013.01.004; RA Ford R.J., Barker A.M., Bakker S.E., Coutts R.H., Ranson N.A., RA Phillips S.E., Pearson A.R., Stockley P.G.; RT "Sequence-specific, RNA-protein interactions overcome electrostatic RT barriers preventing assembly of satellite tobacco necrosis virus coat RT protein."; RL J. Mol. Biol. 425:1050-1064(2013). CC -!- FUNCTION: Self-assembles to form an icosahedral capsid of 17 nm in CC diameter. {ECO:0000269|PubMed:21839089, ECO:0000269|PubMed:23318955, CC ECO:0000269|PubMed:6481804}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:21839089}; CC -!- SUBCELLULAR LOCATION: Virion {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; V01468; CAA24714.1; -; Genomic_RNA. DR PDB; 2BUK; X-ray; 2.45 A; A=1-196. DR PDB; 3S4G; X-ray; 6.00 A; A=1-196. DR PDB; 4BCU; X-ray; 2.29 A; A=1-196. DR PDB; 4V4M; X-ray; 1.45 A; 0/1/2/3/4/5/6/7/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z=1-196. DR PDBsum; 2BUK; -. DR PDBsum; 3S4G; -. DR PDBsum; 4BCU; -. DR PDBsum; 4V4M; -. DR SMR; P03606; -. DR EvolutionaryTrace; P03606; -. DR Proteomes; UP000211161; Segment. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR CDD; cd00259; STNV; 1. DR Gene3D; 2.60.120.20; -; 1. DR InterPro; IPR005597; Satellite_CP-like. DR InterPro; IPR010392; Satellite_virus_coat. DR InterPro; IPR037164; Satellite_virus_coat_sf. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF03898; TNV_CP; 1. DR PIRSF; PIRSF004094; Satellite_CP; 1. DR SUPFAM; SSF88650; Satellite viruses; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Capsid protein; Metal-binding; Reference proteome; KW RNA-binding; Virion. FT CHAIN 1..196 FT /note="Capsid protein" FT /id="PRO_0000222534" FT REGION 1..19 FT /note="RNA-binding" FT /evidence="ECO:0000269|PubMed:23318955" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089, FT ECO:0000269|PubMed:23318955" FT BINDING 65 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089, FT ECO:0000269|PubMed:23318955" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:21839089" FT BINDING 195 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21839089, FT ECO:0000269|PubMed:23318955" FT HELIX 11..23 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 28..38 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 65..78 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:4BCU" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:4BCU" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 125..136 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:2BUK" FT STRAND 143..151 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 154..163 FT /evidence="ECO:0007829|PDB:4BCU" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 172..179 FT /evidence="ECO:0007829|PDB:4BCU" FT STRAND 184..194 FT /evidence="ECO:0007829|PDB:4BCU" SQ SEQUENCE 196 AA; 21715 MW; EE7C4FEA77A2D7A5 CRC64; MAKQQNNRRK SATMRAVKRM INTHLEHKRF ALINSGNTNA TAGTVQNLSN GIIQGDDINQ RSGDQVRIVS HKLHVRGTAI TVSQTFRFIW FRDNMNRGTT PTVLEVLNTA NFMSQYNPIT LQQKRFTILK DVTLNCSLTG ESIKDRIINL PGQLVNYNGA TAVAASNGPG AIFMLQIGDS LVGLWDSSYE AVYTDA //