P0CX57 (YA11A_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 13.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Transposon Ty1-A Gag polyprotein Alternative name(s): Gag-p49 Transposon Ty1 protein A Short name=TY1A Short name=TYA p58 Cleaved into the following 2 chains:
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| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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 structure | Homotrimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Induction | Ty1-A is a weakly expressed element. Induced under amino acid starvation conditions by GCN4. Ref.5 |
| 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). |
| Caution | Transposon Ty1-A (YARCTy1-1) contains a frameshift at position 610, which disrupts the ORF coding for protein TY1B. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Ribosomal frameshifting |
| Ligand | RNA-binding |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome Transposable element |
| Gene Ontology (GO) | |
| Biological_process | transposition, RNA-mediated Inferred from sequence or structural similarity Ref.4. Source: SGD |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell retrotransposon nucleocapsidInferred from sequence or structural similarity Ref.4. Source: SGD |
| Molecular_function | RNA binding Inferred from sequence or structural similarity Ref.4. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 440 | 440 | Transposon Ty1-A Gag polyprotein | PRO_0000278982 | |||||
| Chain | 1 – 401 | 401 | Capsid protein By similarity | PRO_0000278983 | |||||
| Peptide | 402 – 440 | 39 | Gag-p4 By similarity | PRO_0000278984 | |||||
Regions | |||||||||
| Region | 299 – 401 | 103 | RNA-binding By similarity | ||||||
Sites | |||||||||
| Site | 401 – 402 | 2 | Cleavage; by Ty1 protease By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 10 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 16 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 20 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 22 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 23 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 28 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 36 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 71 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 79 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 145 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 160 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 177 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 353 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 371 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 373 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 375 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 405 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 406 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 409 | 1 | Phosphoserine Ref.7 Ref.9 | ||||||
| Modified residue | 411 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 412 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 416 | 1 | Phosphoserine Ref.8 Ref.9 | ||||||
| Modified residue | 418 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 421 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 422 | 1 | Phosphothreonine Ref.9 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region." Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H. Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [2] | "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence." Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F. Genome Res. 8:464-478(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE. |
| [5] | "Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons." Morillon A., Benard L., Springer M., Lesage P. Mol. Cell. Biol. 22:2078-2088(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [6] | "Happy together: the life and times of Ty retrotransposons and their hosts." Lesage P., Todeschini A.L. Cytogenet. Genome Res. 110:70-90(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW. |
| [7] | "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-409 AND SER-411, MASS SPECTROMETRY. Strain: ADR376. |
| [8] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412 AND SER-416, MASS SPECTROMETRY. |
| [9] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-16; SER-20; THR-22; SER-23; THR-28; SER-36; SER-71; SER-79; SER-145; SER-160; SER-280; SER-353; SER-371; SER-373; THR-375; THR-405; SER-406; SER-409; SER-416; SER-418; THR-421 AND THR-422, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L22015 Genomic DNA. Translation: AAC04966.1. BK006935 Genomic DNA. Translation: DAA06992.1. |
| PIR | S40909. |
| RefSeq | NP_009407.1. NM_001178214.1. NP_058192.1. NM_001184393.1. |
3D structure databases | |
| ProteinModelPortal | P0CX57. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YAR010C; YAR010C; YAR010C. YPR137C-A; YPR137C-A; YPR137C-A. |
| GeneID | 851269. 856258. |
| KEGG | sce:YAR010C. sce:YPR137C-A. |
Organism-specific databases | |
| CYGD | YAR010c. |
| SGD | S000000068. YAR010C. |
Phylogenomic databases | |
| HOGENOM | HOG000000740. |
Gene expression databases | |
| ArrayExpress | P0CX57. |
Family and domain databases | |
| InterPro | IPR015820. Retrotransposon_Ty1A_N. [Graphical view] |
| Pfam | PF01021. TYA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 968243. |
Entry information
| Entry name | YA11A_YEAST | ||||||||
| Accession | Primary (citable) accession number: P0CX57 Secondary accession number(s): D6VPM2, O13528 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome I Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names |

Clusters with
