| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Transposon Ty1-H Gag polyprotein
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| http://www.biopax.org/relea... |
YH11A_YEAST
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
CA,
Capsid protein,
Gag-p4,
Gag-p45,
Gag-p49,
TY1A,
TYA,
Transposon Ty1 protein A,
p54,
p58
|
| http://www.biopax.org/relea... |
FUNCTION: 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 Ty1 RNA and initiation of reverse transcription (By similarity). SUBUNIT: Homotrimer (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). ALTERNATIVE PRODUCTS: Event=Ribosomal frameshifting; Named isoforms=2; Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity); Name=Transposon Ty1-H Gag polyprotein; IsoId=P0C2I4-1; Sequence=Displayed; Note=Produced by conventional translation; Name=Transposon Ty1-H Gag-Pol polyprotein; IsoId=O13535-1; Sequence=External; Note=Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YHR214C-C ORF; DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities (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). GENE SYNONYMS: YHRCTy1-1 GAG. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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