UniProt functional annotation for P03612



	UniProt functional annotation for P03612

UniProt code: P03612.

Organism: Escherichia phage MS2 (Bacteriophage MS2).

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

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:8254664, PubMed:18662904). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:9469847, PubMed:26608810, PubMed:7523953). The capsid contains also 1 copy of the A2 maturation protein (PubMed:8254664). {ECO:0000269|PubMed:12948491, ECO:0000269|PubMed:18662904, ECO:0000269|PubMed:26608810, ECO:0000269|PubMed:7523953, ECO:0000269|PubMed:9469847, ECO:0000305|PubMed:8254664}.

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:16531233, ECO:0000269|PubMed:9207028, ECO:0000269|PubMed:9245600}.

Subunit: Homodimer (PubMed:8254664, PubMed:7788292, PubMed:19521994). The capsid proteins form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers (PubMed:8254664). 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:12948491). {ECO:0000269|PubMed:19521994, ECO:0000269|PubMed:7788292, ECO:0000269|PubMed:8254664, ECO:0000305|PubMed:12948491}.

Subcellular location: Virion {ECO:0000269|PubMed:8254664}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000269|PubMed:23810697, ECO:0000305|PubMed:8254664}.

Similarity: Belongs to the Levivirus capsid protein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia phage MS2 (Bacteriophage MS2).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Lenarviricota; Allassoviricetes; Levivirales; Leviviridae; Levivirus.



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:8254664, PubMed:18662904). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:9469847, PubMed:26608810, PubMed:7523953). The capsid contains also 1 copy of the A2 maturation protein (PubMed:8254664). {ECO:0000269\|PubMed:12948491, ECO:0000269\|PubMed:18662904, ECO:0000269\|PubMed:26608810, ECO:0000269\|PubMed:7523953, ECO:0000269\|PubMed:9469847, ECO:0000305\|PubMed:8254664}.



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:16531233, ECO:0000269\|PubMed:9207028, ECO:0000269\|PubMed:9245600}.


Subunit:		Homodimer (PubMed:8254664, PubMed:7788292, PubMed:19521994). The capsid proteins form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers (PubMed:8254664). 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:12948491). {ECO:0000269\|PubMed:19521994, ECO:0000269\|PubMed:7788292, ECO:0000269\|PubMed:8254664, ECO:0000305\|PubMed:12948491}.
Subcellular location:		Virion {ECO:0000269\|PubMed:8254664}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000269\|PubMed:23810697, ECO:0000305\|PubMed:8254664}.
Similarity:		Belongs to the Levivirus capsid protein family. {ECO:0000305}.