COAT_PHMV
ID COAT_PHMV Reviewed; 188 AA.
AC P36351;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: 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.
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).
CC -!- SUBUNIT: The virus coat is composed of 180 copies of the coat protein
CC arranged in an icosahedral shell.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tymoviruses coat protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty
CC capsid structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1e57";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qjz";
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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 PDBsum; 1E57; -.
DR PDBsum; 1QJZ; -.
DR PDBsum; 2WWS; -.
DR PDBsum; 2XPJ; -.
DR SMR; P36351; -.
DR GeneID; 940246; -.
DR KEGG; vg:940246; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..188
FT /note="Coat protein"
FT /id="PRO_0000222925"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2XPJ"
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