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P25383 (YC21A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transposon Ty2-C Gag polyprotein
Alternative name(s):
Transposon Ty2 protein A
Short name=TY2A
Short name=TYA
Ty1-17 protein A

Cleaved into the following 2 chains:

  1. Capsid protein
    Short name=CA
  2. Gag-p4
Gene names
Name:TY2A-C
Synonyms:YCLWTy2-1 GAG
Ordered Locus Names:YCL020W
ORF Names:YCL20W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 Ty2 RNA and initiation of reverse transcription By similarity.

Subunit structure

Homotrimer By similarity.

Subcellular location

Cytoplasm By similarity.

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. Ty2 retrotransposons belong to the copia elements (pseudoviridae).

Ontologies

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift.
Isoform Transposon Ty2-C Gag polyprotein (identifier: P25383-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by conventional translation.
Isoform Transposon Ty2-C Gag-Pol polyprotein (identifier: P25384-1)

The sequence of this isoform can be found in the external entry P25384.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YCL020W ORF.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Transposon Ty2-C Gag polyprotein
PRO_0000203495
Chain1 – 397397Capsid protein By similarity
PRO_0000279282
Peptide398 – 43841Gag-p4 By similarity
PRO_0000279283

Regions

Region295 – 397103RNA-binding By similarity

Sites

Site397 – 3982Cleavage; by Ty2 protease By similarity

Experimental info

Sequence conflict1741E → D Ref.1
Sequence conflict1741E → D in CAA27457. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Transposon Ty2-C Gag polyprotein [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: D92E6A7BDA32A5B4

FASTA43849,841
        10         20         30         40         50         60 
MESQQLHQNP RSLHGSAYAS VTSKEVPSNQ DPLAVSASNL PEFDRDSTKV NSQQETTPGT 

        70         80         90        100        110        120 
SAVPENHHHV SPQPASVPPP QNGQYQQHGM MTPNKAMASN WAHYQQPSMM TCSHYQTSPA 

       130        140        150        160        170        180 
YYQPDPHYPL PQYIPPLSTS SPDPIDSQNQ HSEVPQAETK VRNNVLPPHT LTSEENFSTW 

       190        200        210        220        230        240 
VKFYIRFLKN SNLGDIIPND QGEIKRQMTY EEHAYIYNTF QAFAPFHLLP TWVKQILEIN 

       250        260        270        280        290        300 
YADILTVLCK SVSKMQTNNQ ELKDWIALAN LEYDGSTSAD TFEITVSTII QRLKENNINV 

       310        320        330        340        350        360 
SDRLACQLIL KGLSGDFKYL RNQYRTKTNM KLSQLFAEIQ LIYDENKIMN LNKPSQYKQH 

       370        380        390        400        410        420 
SEYKNVSRTS PNTTNTKVTT RNYQRTNSSK PRAAKAHNIA TSSKFSRVNN DHINESTVSS 

       430 
QYLSDDNELS LRPATERI 

« Hide

Isoform Transposon Ty2-C Gag-Pol polyprotein [UniParc].

See P25384.

References

« Hide 'large scale' references
[1]"A 'hot-spot' for Ty transposition on the left arm of yeast chromosome III."
Warmington J.R., Anwar R., Newlon C.S., Waring R.B., Davies R.W., Indge K.J., Oliver S.G.
Nucleic Acids Res. 14:3475-3485(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence characterization of Ty 1-17, a class II transposon from yeast."
Warmington J.R., Waring R.B., Newlon C.S., Indge K.J., Oliver S.G.
Nucleic Acids Res. 13:6679-6693(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Variants within the yeast Ty sequence family encode a class of structurally conserved proteins."
Fulton A.M., Mellor J., Dobson M.J., Chester J., Warmington J.R., Indge K.J., Oliver S.G., de la Paz P., Wilson W., Kingsman A.J., Kingsman S.M.
Nucleic Acids Res. 13:4097-4112(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MD 40-4C.
[4]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Expression of Ty-lacZ fusions in Saccharomyces cerevisiae."
Bowen B.A., Fulton A.M., Tuite M.F., Kingsman S.M., Kingsman A.J.
Nucleic Acids Res. 12:1627-1640(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
[8]"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.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03840 Genomic DNA. Translation: CAA27457.1.
X59720 Genomic DNA. Translation: CAA42364.2.
X02546 Genomic DNA. Translation: CAA26398.1.
X00394 Genomic DNA. Translation: CAA25113.1.
BK006937 Genomic DNA. Translation: DAA07464.1.
PIRS19347.
RefSeqNP_009910.2. NM_001178667.1. [P25383-1]

3D structure databases

ProteinModelPortalP25383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30963. 7 interactions.
DIPDIP-7334N.
IntActP25383. 4 interactions.
MINTMINT-406398.
STRING4932.YCL020W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL020W; YCL020W; YCL020W. [P25383-1]
GeneID850339.
KEGGsce:YCL020W.

Organism-specific databases

CYGDYCL020w.
SGDS000000525. YCL020W.

Phylogenomic databases

GeneTreeENSGT00730000111602.
HOGENOMHOG000000740.
OrthoDBEOG7TJ3S3.

Gene expression databases

GenevestigatorP25383.

Family and domain databases

InterProIPR015820. Retrotransposon_Ty1A_N.
[Graphical view]
PfamPF01021. TYA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965780.

Entry information

Entry nameYC21A_YEAST
AccessionPrimary (citable) accession number: P25383
Secondary accession number(s): D6VQZ5, Q07125
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 26, 2001
Last modified: May 14, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD