ID CAPSD_PHMV Reviewed; 188 AA. AC P36351; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 10-JUN-2026, entry version 89. DE RecName: Full=Capsid protein; DE AltName: Full=Coat protein; DE AltName: Full=Virion protein; OS Physalis mottle virus (PhMV) (Belladonna mottle virus-Iowa). OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes; OC Tymovirales; Tymoviridae; Tymovirus; Tymovirus physalis. OX NCBI_TaxID=72539; OH NCBI_TaxID=304155; Physalis heterophylla. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1562236; DOI=10.1007/bf01317270; RA Jacob A.N.K., Murthy M.R., Savithri H.S.; RT "Nucleotide sequence of the 3' terminal region of belladonna mottle virus- RT Iowa (renamed Physalis mottle virus) RNA and an analysis of the RT relationships of tymoviral coat proteins."; RL Arch. Virol. 123:367-377(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=8460497; DOI=10.1006/viro.1993.1205; RA Kekuda R., Karande A.A., Jacob A.N.K., Savithri H.S.; RT "Architecture of physalis mottle tymovirus as probed by monoclonal RT antibodies and cross-linking studies."; RL Virology 193:959-966(1993). RN [3] {ECO:0007744|PDB:1QJZ} RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10369772; DOI=10.1006/jmbi.1999.2787; RA Krishna S.S., Hiremath C.N., Munshi S.K., Prahadeeswaran D., Sastri M., RA Savithri H.S., Murthy M.R.; RT "Three-dimensional structure of physalis mottle virus: implications for the RT viral assembly."; RL J. Mol. Biol. 289:919-934(1999). RN [4] {ECO:0007744|PDB:1E57} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS). RX PubMed=11286554; DOI=10.1006/jmbi.2001.4533; RA Krishna S.S., Sastri M., Savithri H.S., Murthy M.R.; RT "Structural studies on the empty capsids of Physalis mottle virus."; RL J. Mol. Biol. 307:1035-1047(2001). RN [5] {ECO:0007744|PDB:2WWS, ECO:0007744|PDB:2XPJ} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS). RA Sagurthi S.R., Rajaram V., Savithri H.S., Murthy M.R.N.; RT "Crystal Structure of Natural Bottom Component of Phmv."; RL Submitted (AUG-2010) to the PDB data bank. CC -!- FUNCTION: Self-assembles to form a T=3 icosahedral capsid composed of CC 180 copies of the capsid protein. The capsid encapsulates the single- CC stranded RNA genome. {ECO:0000250|UniProtKB:P20125}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P20125}. CC -!- SIMILARITY: Belongs to the tymoviruses capsid protein family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty CC capsid structure; CC URL="https://viperdb.org/Info_Page.php?VDB=1e57"; CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid CC structure; CC URL="https://viperdb.org/Info_Page.php?VDB=1qjz"; 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; S97776; AAB21997.1; -; Genomic_RNA. DR PIR; B45540; B45540. DR RefSeq; NP_619757.1; NC_003634.1. DR PDB; 1E57; X-ray; 3.20 A; A/B/C=1-188. DR PDB; 1QJZ; X-ray; 3.80 A; A/B/C=1-188. DR PDB; 2WWS; X-ray; 3.90 A; A/B/C=1-188. DR PDB; 2XPJ; X-ray; 3.40 A; A/B/C=1-188. DR SMR; P36351; -. DR GeneID; 940246; -. DR KEGG; vg:940246; -. DR OrthoDB; 15633at10239; -. DR EvolutionaryTrace; P36351; -. DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR Gene3D; 2.60.120.20; -; 1. DR InterPro; IPR000574; Tymo_coat. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF00983; Tymo_coat; 1. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1. DR PDBsum; 1E57; -. DR PDBsum; 1QJZ; -. DR PDBsum; 2WWS; -. DR PDBsum; 2XPJ; -. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; T=3 icosahedral capsid protein; Virion. FT CHAIN 1..188 FT /note="Capsid protein" FT /id="PRO_0000222925" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:2XPJ" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:1E57" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:1E57" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1E57" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 91..101 FT /evidence="ECO:0007829|PDB:1E57" FT TURN 105..109 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 135..138 FT /evidence="ECO:0007829|PDB:2XPJ" FT STRAND 142..146 FT /evidence="ECO:0007829|PDB:2XPJ" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:1E57" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:1E57" SQ SEQUENCE 188 AA; 19974 MW; D1DC64831FF5DC61 CRC64; MDSSEVVKVK QASIPAPGSI LSQPNTEQSP AIVLPFQFEA TTFGTAETAA QVSLQTADPI TKLTAPYRHA QIVECKAILT PTDLAVSNPL TVYLAWVPAN SPATPTQILR VYGGQSFVLG GAISAAKTIE VPLNLDSVNR MLKDSVTYTD TPKLLAYSRA PTNPSKIPTA SIQISGRIRL SKPMLIAN //