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Protein

Capsid protein

Gene
N/A
Organism
Enterobacteria phage GA (Bacteriophage GA)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein.By similarity
Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.By similarity

GO - Molecular functioni

Keywordsi

Molecular functionRNA-binding
Biological processTranslation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid protein
Short name:
CP
Alternative name(s):
Coat protein
OrganismiEnterobacteria phage GA (Bacteriophage GA)
Taxonomic identifieri12018 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageLeviviridaeLevivirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000002126 Componenti: Genome

Subcellular locationi

  • Virion By similarity

  • Note: The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, T=3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00001648412 – 130Capsid proteinAdd BLAST129

Interactioni

Subunit structurei

Homodimer. The capsid proteins form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers. The homodimers binds to the viral RNA via an operator hairpin, but also to many other RNA sequences in the viral genome; this interaction probably shifts the virus from the replicative to the assembly phase and ensures specific encapsidation of the viral genome.By similarity

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Beta strandi12 – 16Combined sources5
Beta strandi18 – 24Combined sources7
Helixi26 – 28Combined sources3
Beta strandi30 – 36Combined sources7
Helixi38 – 40Combined sources3
Beta strandi43 – 51Combined sources9
Turni52 – 54Combined sources3
Beta strandi55 – 65Combined sources11
Beta strandi83 – 93Combined sources11
Helixi102 – 111Combined sources10
Helixi117 – 124Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GAVX-ray3.400/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i2-130[»]
1UNAX-ray2.80A/B2-130[»]
ProteinModelPortaliP07234.
SMRiP07234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07234.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni31 – 104Viral RNA-bindingBy similarityAdd BLAST74

Family and domain databases

Gene3Di3.30.380.10. 1 hit.
InterProiView protein in InterPro
IPR002703. Levivir_coat.
IPR015954. Phage_RNA-type_capsid.
PfamiView protein in Pfam
PF01819. Levi_coat. 1 hit.
SUPFAMiSSF55405. SSF55405. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P07234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLRSFVLV DNGGTGNVTV VPVSNANGVA EWLSNNSRSQ AYRVTASYRA
60 70 80 90 100
SGADKRKYAI KLEVPKIVTQ VVNGVELPGS AWKAYASIDL TIPIFAATDD
110 120 130
VTVISKSLAG LFKVGNPIAE AISSQSGFYA
Length:130
Mass (Da):13,683
Last modified:January 23, 2007 - v3
Checksum:i4FBB64DCC866CDA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03869 mRNA. Translation: CAA27497.1.
PIRiA29178. VCBPGA.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure with 4 residue deletion FG loop

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03869 mRNA. Translation: CAA27497.1.
PIRiA29178. VCBPGA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GAVX-ray3.400/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i2-130[»]
1UNAX-ray2.80A/B2-130[»]
ProteinModelPortaliP07234.
SMRiP07234.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07234.

Family and domain databases

Gene3Di3.30.380.10. 1 hit.
InterProiView protein in InterPro
IPR002703. Levivir_coat.
IPR015954. Phage_RNA-type_capsid.
PfamiView protein in Pfam
PF01819. Levi_coat. 1 hit.
SUPFAMiSSF55405. SSF55405. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCAPSD_BPGA
AccessioniPrimary (citable) accession number: P07234
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: February 15, 2017
This is version 94 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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 one 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.