UniProt functional annotation for P03615



	UniProt functional annotation for P03615

UniProt code: P03615.

Organism: Escherichia virus Qbeta (Bacteriophage Q-beta).

Taxonomy: Viruses; Riboviria; Orthornavirae; Lenarviricota; Allassoviricetes; Levivirales; Leviviridae; Allolevivirus.

Function: 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) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640). {ECO:0000269|PubMed:19913556, ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:8943226}.

Function: 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. {ECO:0000269|PubMed:8943226}.

Subunit: Homodimer (PubMed:16531233). 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 (PubMed:8943226, PubMed:16531233). Interacts with the maturation protein A2 (PubMed:28111107, PubMed:29078304). {ECO:0000269|PubMed:16531233, ECO:0000269|PubMed:28111107, ECO:0000269|PubMed:29078304, ECO:0000269|PubMed:8943226}.

Subcellular location: Virion {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. Note=The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein. {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia virus Qbeta (Bacteriophage Q-beta).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Lenarviricota; Allassoviricetes; Levivirales; Leviviridae; Allolevivirus.



Function:		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) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640). {ECO:0000269\|PubMed:19913556, ECO:0000269\|PubMed:27671640, ECO:0000269\|PubMed:8943226}.



Function:		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. {ECO:0000269\|PubMed:8943226}.


Subunit:		Homodimer (PubMed:16531233). 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 (PubMed:8943226, PubMed:16531233). Interacts with the maturation protein A2 (PubMed:28111107, PubMed:29078304). {ECO:0000269\|PubMed:16531233, ECO:0000269\|PubMed:28111107, ECO:0000269\|PubMed:29078304, ECO:0000269\|PubMed:8943226}.
Subcellular location:		Virion {ECO:0000269\|PubMed:27671640, ECO:0000269\|PubMed:29078304}. Note=The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein. {ECO:0000269\|PubMed:27671640, ECO:0000269\|PubMed:29078304}.