FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP (By similarity).
FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro- elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).
FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity). CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- phosphomonoester.
SUBUNIT: The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).
SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
ALTERNATIVE PRODUCTS: Event=Ribosomal frameshifting; Named isoforms=2; Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift between the codons for Leu-435 and Gly-436. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity); Name=Transposon Ty1-LR1 Gag-Pol polyprotein; IsoId=Q12088-1; Sequence=Displayed; Note=Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR035C-B ORF; Name=Transposon Ty1-LR1 Gag polyprotein; IsoId=P0CX68-1; Sequence=External; Note=Produced by conventional translation;
DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities (By similarity).
DOMAIN: Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'- processing and strand transfer activities of purified integrase protein (By similarity).
PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). MISCELLANEOUS: 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. Ty1 retrotransposons belong to the copia elements (pseudoviridae).
SIMILARITY: Contains 1 integrase catalytic domain.
SIMILARITY: Contains 1 peptidase A11 domain.
SIMILARITY: Contains 1 reverse transcriptase Ty1/copia-type domain.
SIMILARITY: Contains 1 RNase H Ty1/copia-type domain.
SEQUENCE CAUTION: Sequence=DAA09354.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
GENE SYNONYMS: YLRCTy1-1 POL.
COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.