CAPSD_STNV1
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 03-AUG-2022, entry version 113.
DE RecName: Full=Capsid protein {ECO:0000305};
DE AltName: Full=Coat protein {ECO:0000305};
OS Satellite tobacco necrosis virus 1.
OC Viruses; Riboviria; Albetovirus.
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; Genome.
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; SSF88650; 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
