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CAPSD_TBSVB
ID   CAPSD_TBSVB             Reviewed;         388 AA.
AC   P11795; Q9IW10;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE   AltName: Full=p41;
GN   ORFNames=ORF2;
OS   Tomato bushy stunt virus (strain BS-3) (TBSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Tombusvirus.
OX   NCBI_TaxID=12146;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=3749; Malus.
OH   NCBI_TaxID=3766; Pyrus (pears).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4111; Solanum melongena (Eggplant) (Aubergine).
OH   NCBI_TaxID=29777; Tolmiea menziesii.
OH   NCBI_TaxID=13305; Tulipa.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Galetzka D., Russo M., Rubino L., Krczal G.;
RT   "Molecular characterization of a tombusvirus associated with a disease of
RT   statice (Goniolimon tataricum (L.) Boiss.).";
RL   J. Plant Pathol. 82:151-155(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-388.
RX   PubMed=6481803; DOI=10.1016/0022-2836(84)90045-7;
RA   Hopper P., Harrison S.C., Sauer R.T.;
RT   "Structure of tomato bushy stunt virus. V. Coat protein sequence
RT   determination and its structural implications.";
RL   J. Mol. Biol. 177:701-713(1984).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=6644820; DOI=10.1016/s0022-2836(83)80314-3;
RA   Olson A.J., Bricogne G., Harrison S.C.;
RT   "Structure of tomato bushy stunt virus IV. The virus particle at 2.9-A
RT   resolution.";
RL   J. Mol. Biol. 171:61-93(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=19711552; DOI=10.1038/276368a0;
RA   Harrison S.C., Olson A.J., Schutt C.E., Winkler F.K., Bricogne G.;
RT   "Tomato bushy stunt virus at 2.9 A resolution.";
RL   Nature 276:368-373(1978).
CC   -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC       with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180
CC       capsid proteins.
CC   -!- SUBUNIT: Homomultimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2tbv";
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DR   EMBL; AJ271328; CAB66390.1; -; mRNA.
DR   PIR; S07259; S07259.
DR   PDB; 2TBV; X-ray; 2.90 A; A/B/C=2-388.
DR   PDBsum; 2TBV; -.
DR   SMR; P11795; -.
DR   EvolutionaryTrace; P11795; -.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; 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; 2.60.120.20; -; 1.
DR   InterPro; IPR000937; Capsid_prot_S-dom_vir.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00729; Viral_coat; 1.
DR   PRINTS; PR00233; ICOSAHEDRAL.
DR   PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; RNA-binding;
KW   T=3 icosahedral capsid protein; Virion.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..388
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222866"
FT   REGION          2..102
FT                   /note="R domain, interaction with RNA"
FT   REGION          57..63
FT                   /note="Involved in encapsidation"
FT                   /evidence="ECO:0000250"
FT   REGION          103..264
FT                   /note="S domain, virion shell"
FT   REGION          265..388
FT                   /note="P domain, projecting"
FT   CONFLICT        14
FT                   /note="I -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34..36
FT                   /note="HIS -> YIG (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="T -> TG (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="L -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="I -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="H -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249..250
FT                   /note="TN -> AD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254..259
FT                   /note="DVFISY -> ELFLAR (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275..276
FT                   /note="TR -> SK (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="V -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="A -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366..380
FT                   /note="TTGISSATVNVVRGT -> VSGVAAGILLVGRA (in Ref. 2; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          109..116
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          119..123
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          151..168
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   HELIX           192..195
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   TURN            231..234
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          240..245
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          251..263
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          304..308
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          310..319
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          325..331
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          333..340
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          343..345
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          347..355
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          360..365
FT                   /evidence="ECO:0007829|PDB:2TBV"
FT   STRAND          371..376
FT                   /evidence="ECO:0007829|PDB:2TBV"
SQ   SEQUENCE   388 AA;  40911 MW;  008DF490F253B79E CRC64;
     MAMTTRNNNN VLAISKKQLG VLAASAAVGA LRNHISESSP ALLQSAVGLG KKALNKVRNR
     RKQGNQQIIT HVGGVGGSIM APVAVSRQLV GSKPKFTGRT SGSVTVTHRE YLTQVNNSSG
     FVVNGGIVGN LLQLNPSNGT LFSWLPAIAS NFDQYSFNSV VLHYVPLCGT TEVGRVALYF
     DKDSQDPEPA DRVELANFGV LKETAPWAEA MLRIPTDKVK RYCNDSATVD QKLIDLGQLG
     IATYGGAGTN AVGDVFISYS VTLYFPQPTN TLLSTRRLDL TGSLADATGP GYLVLTRTPT
     VLTHTFRVTG TFNLSGGLRC LTSLTLGATG AVVINDILAI DNVGTASAYF LNCTVSSLPA
     TVTFTTTGIS SATVNVVRGT RANVVNLL
 
 
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