ID   CAPSD_TAV               Reviewed;         229 AA.
AC   P23627;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   02-JUN-2021, entry version 88.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF3b;
OS   Tomato aspermy virus (TAV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12315;
OH   NCBI_TaxID=4627; Canna.
OH   NCBI_TaxID=41568; Chrysanthemum morifolium (Florist's daisy) (Dendranthema grandiflorum).
OH   NCBI_TaxID=4688; Lilium.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Chrysanthemum isolate;
RX   PubMed=1990057; DOI=10.1099/0022-1317-72-1-1;
RA   O'Reilly D., Thomas C.J.R., Coutts R.H.A.;
RT   "Tomato aspermy virus has an evolutionary relationship with other
RT   tripartite RNA plant viruses.";
RL   J. Gen. Virol. 72:1-7(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-212, AND DISULFIDE BOND.
RX   PubMed=7784430; DOI=10.1002/prot.340210310;
RA   Canady M.A., Leja C.A., Day J., McPherson A.;
RT   "Preliminary X-ray diffraction analysis of crystals of tomato aspermy virus
RT   (TAV).";
RL   Proteins 21:265-267(1995).
CC   -!- FUNCTION: Capsid protein. Probably binds RNA and plays a role in
CC       packaging (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal arginine-rich stretch does not seem to be the
CC       major RNA-binding region that allows formation of an infectious
CC       ribonucleoprotein complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cucumovirus capsid protein family.
CC       {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; D01015; BAA00820.1; -; Genomic_RNA.
DR   PIR; B54334; JQ0928.
DR   PDB; 1LAJ; X-ray; 3.40 A; A/B/C=1-212.
DR   PDBsum; 1LAJ; -.
DR   SMR; P23627; -.
DR   EvolutionaryTrace; P23627; -.
DR   Proteomes; UP000007399; Genome.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; 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; 2.60.120.530; -; 1.
DR   InterPro; IPR000247; Cucumovirus_coat.
DR   InterPro; IPR023800; Cucumovirus_coat_A.
DR   InterPro; IPR037137; Cucumovirus_coat_Asu_sf.
DR   Pfam; PF00760; Cucumo_coat; 1.
DR   PRINTS; PR00222; CUCUMOCOAT.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Capsid protein; Disulfide bond;
KW   Reference proteome; Ribonucleoprotein; RNA-binding;
KW   T=3 icosahedral capsid protein; Viral nucleoprotein; Virion.
FT   CHAIN           1..229
FT                   /note="Capsid protein"
FT                   /id="PRO_0000083224"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; by host"
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..106
FT                   /evidence="ECO:0000269|PubMed:7784430"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          85..89
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   TURN            94..98
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          102..113
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   HELIX           178..182
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          184..192
FT                   /evidence="ECO:0007829|PDB:1LAJ"
FT   STRAND          198..208
FT                   /evidence="ECO:0007829|PDB:1LAJ"
SQ   SEQUENCE   229 AA;  25753 MW;  722DB100FF6D4F26 CRC64;
     MAQNGTGGGS RRPRRGRRNN NNNNSTARDK ALLALTQQVN RLANIASSSA PSLQHPTFIA
     SKKCRAGYTY TSLDVRPTRT EKDKSFGQRL IIPVPVSEYP KKKVSCVQVR LNPSPKFNST
     IWVSLRRLDE TTLLTSENVF KLFTDGLAAV LIYQHVPTGI QPNNKITFDM SNVGAEIGDM
     GKYALIVYSK DDVLEADEMV IHIDIEHQRI PSLQRSRCDS TRMHDVRRR