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Protein

Capsid protein

Gene

ORF2

Organism
Tomato bushy stunt virus (strain BS-3) (TBSV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. structural molecule activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid protein
Alternative name(s):
Coat protein
p41
Gene namesi
ORF Names:ORF2
OrganismiTomato bushy stunt virus (strain BS-3) (TBSV)
Taxonomic identifieri12146 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTombusviridaeTombusvirus
Virus hostiCapsicum annuum (Bell pepper) [TaxID: 4072]
Malus [TaxID: 3749]
Pyrus (pears) [TaxID: 3766]
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]
Solanum melongena (Eggplant) (Aubergine) [TaxID: 4111]
Tolmiea menziesii [TaxID: 29777]
Tulipa [TaxID: 13305]

Subcellular locationi

  1. Virion Curated

GO - Cellular componenti

  1. T=3 icosahedral viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, T=3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 388387Capsid proteinPRO_0000222866Add
BLAST

Post-translational modificationi

The N-terminus is blocked.Curated

Interactioni

Subunit structurei

Homomultimer.Curated

Structurei

Secondary structure

1
388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi109 – 1168Combined sources
Beta strandi119 – 1235Combined sources
Turni124 – 1263Combined sources
Beta strandi134 – 1363Combined sources
Helixi145 – 1473Combined sources
Turni148 – 1503Combined sources
Beta strandi151 – 16818Combined sources
Helixi192 – 1954Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi224 – 2263Combined sources
Turni231 – 2344Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi251 – 26313Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi304 – 3085Combined sources
Beta strandi310 – 31910Combined sources
Beta strandi325 – 3317Combined sources
Beta strandi333 – 3408Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi347 – 3559Combined sources
Beta strandi360 – 3656Combined sources
Beta strandi371 – 3766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2TBVX-ray2.90A/B/C2-388[»]
ProteinModelPortaliP11795.
SMRiP11795. Positions 68-388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11795.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 102101R domain, interaction with RNAAdd
BLAST
Regioni57 – 637Involved in encapsidationBy similarity
Regioni103 – 264162S domain, virion shellAdd
BLAST
Regioni265 – 388124P domain, projectingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 104Poly-Asn

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.20. 1 hit.
InterProiIPR000937. Capsid_prot_S-dom_vir.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00729. Viral_coat. 1 hit.
[Graphical view]
PRINTSiPR00233. ICOSAHEDRAL.
PROSITEiPS00555. ICOSAH_VIR_COAT_S. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMTTRNNNN VLAISKKQLG VLAASAAVGA LRNHISESSP ALLQSAVGLG
60 70 80 90 100
KKALNKVRNR RKQGNQQIIT HVGGVGGSIM APVAVSRQLV GSKPKFTGRT
110 120 130 140 150
SGSVTVTHRE YLTQVNNSSG FVVNGGIVGN LLQLNPSNGT LFSWLPAIAS
160 170 180 190 200
NFDQYSFNSV VLHYVPLCGT TEVGRVALYF DKDSQDPEPA DRVELANFGV
210 220 230 240 250
LKETAPWAEA MLRIPTDKVK RYCNDSATVD QKLIDLGQLG IATYGGAGTN
260 270 280 290 300
AVGDVFISYS VTLYFPQPTN TLLSTRRLDL TGSLADATGP GYLVLTRTPT
310 320 330 340 350
VLTHTFRVTG TFNLSGGLRC LTSLTLGATG AVVINDILAI DNVGTASAYF
360 370 380
LNCTVSSLPA TVTFTTTGIS SATVNVVRGT RANVVNLL
Length:388
Mass (Da):40,911
Last modified:October 5, 2010 - v2
Checksum:i008DF490F253B79E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141I → V AA sequence (PubMed:6481803).Curated
Sequence conflicti34 – 363HIS → YIG AA sequence (PubMed:6481803).Curated
Sequence conflicti107 – 1071T → TG AA sequence (PubMed:6481803).Curated
Sequence conflicti131 – 1311L → S AA sequence (PubMed:6481803).Curated
Sequence conflicti148 – 1481I → L AA sequence (PubMed:6481803).Curated
Sequence conflicti163 – 1631H → D AA sequence (PubMed:6481803).Curated
Sequence conflicti249 – 2502TN → AD AA sequence (PubMed:6481803).Curated
Sequence conflicti254 – 2596DVFISY → ELFLAR AA sequence (PubMed:6481803).Curated
Sequence conflicti275 – 2762TR → SK AA sequence (PubMed:6481803).Curated
Sequence conflicti308 – 3081V → A AA sequence (PubMed:6481803).Curated
Sequence conflicti348 – 3481A → D AA sequence (PubMed:6481803).Curated
Sequence conflicti366 – 38015TTGIS…VVRGT → VSGVAAGILLVGRA AA sequence (PubMed:6481803).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271328 mRNA. Translation: CAB66390.1.
PIRiS07259.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271328 mRNA. Translation: CAB66390.1.
PIRiS07259.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2TBVX-ray2.90A/B/C2-388[»]
ProteinModelPortaliP11795.
SMRiP11795. Positions 68-388.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11795.

Family and domain databases

Gene3Di2.60.120.20. 1 hit.
InterProiIPR000937. Capsid_prot_S-dom_vir.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00729. Viral_coat. 1 hit.
[Graphical view]
PRINTSiPR00233. ICOSAHEDRAL.
PROSITEiPS00555. ICOSAH_VIR_COAT_S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of a tombusvirus associated with a disease of statice (Goniolimon tataricum (L.) Boiss.)."
    Galetzka D., Russo M., Rubino L., Krczal G.
    J. Plant Pathol. 82:151-155(2000)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of tomato bushy stunt virus. V. Coat protein sequence determination and its structural implications."
    Hopper P., Harrison S.C., Sauer R.T.
    J. Mol. Biol. 177:701-713(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-388.
  3. "Structure of tomato bushy stunt virus IV. The virus particle at 2.9-A resolution."
    Olson A.J., Bricogne G., Harrison S.C.
    J. Mol. Biol. 171:61-93(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  4. "Tomato bushy stunt virus at 2.9 A resolution."
    Harrison S.C., Olson A.J., Schutt C.E., Winkler F.K., Bricogne G.
    Nature 276:368-373(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Entry informationi

Entry nameiCAPSD_TBSVB
AccessioniPrimary (citable) accession number: P11795
Secondary accession number(s): Q9IW10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: November 26, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.