Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription (By similarity). Homotrimer. The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty2 retrotransposons belong to the copia elements (pseudoviridae). Could be the product of a pseudogene unlikely to encode a functional protein. Transposon Ty2-GR1 (YGRCTy2-1) has a stop codon at position 28, which disrupts the gene coding for this protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set. Truncated C-terminus. Truncated C-terminus.