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Q03964 (YD17A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transposon Ty1-DR2 Gag polyprotein
Alternative name(s):
Gag-p49
Transposon Ty1 protein A
Short name=TY1A
Short name=TYA
p58

Cleaved into the following 2 chains:

  1. Capsid protein
    Short name=CA
    Alternative name(s):
    Gag-p45
    p54
  2. Gag-p4
Gene names
Name:TY1A-DR2
Ordered Locus Names:YDR170W-A
ORF Names:YD9395.02
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length440 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 Ty1 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. Ty1 retrotransposons belong to the copia elements (pseudoviridae).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Transposon Ty1-DR2 Gag polyprotein
PRO_0000279040
Chain1 – 401401Capsid protein By similarity
PRO_0000279041
Peptide402 – 44039Gag-p4 By similarity
PRO_0000279042

Regions

Region299 – 401103RNA-binding By similarity

Sites

Site401 – 4022Cleavage; by Ty1 protease By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03964 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5E10CEE8878CD80E

FASTA44049,445
        10         20         30         40         50         60 
MESQQLSQHS PISHGSACAS VTSKEVQTTQ DPLDISASKT EECEKVFTQA NSQQPTTPPS 

        70         80         90        100        110        120 
AAVPENHHHA SPQAAQVPLP QNGPYPQQRM MTPQQANISG WPVYGHPSLM PYPPYQMSPM 

       130        140        150        160        170        180 
YAPPGAQSQF TQYPQYVGTH LNTPSPESGN SFPDSSSAKS NMTSTNQHVR PPPILTSPND 

       190        200        210        220        230        240 
FLNWVKIYIK FLQNSNLGDI IPTATRKAVR QMTDDELTFL CHTFQLFALS QFLPTWVKDI 

       250        260        270        280        290        300 
LSVDYTDIMK ILSKSINKMQ SDTQEVNDIT TLANLHYNGS TPADAFEAEV TNILDRLKNN 

       310        320        330        340        350        360 
GIPINNKVAC QFIMRGLSGE YKFLRYARHR YIHMTVADLF SDIHSMYEEQ QESKRNKSTY 

       370        380        390        400        410        420 
RRSPSDEKKD SRTYTNTTKP KSITRNSQKP NNSQSRTARA HNVSTSNNFP GPDNDLIRGS 

       430        440 
TTEPIQLKNK HDLHLRPGTY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46727 Genomic DNA. Translation: CAA86697.1.
BK006938 Genomic DNA. Translation: DAA12012.1.
PIRS49765.
RefSeqNP_010455.1. NM_001184320.1.

3D structure databases

ProteinModelPortalQ03964.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32223. 9 interactions.
DIPDIP-8799N.
IntActQ03964. 2 interactions.
MINTMINT-680391.
STRING4932.YDR170W-A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR170W-A; YDR170W-A; YDR170W-A.
GeneID851750.
KEGGsce:YDR170W-A.

Organism-specific databases

CYGDYDR170w-a.
SGDS000007227. YDR170W-A.

Phylogenomic databases

GeneTreeENSGT00710000106943.
HOGENOMHOG000000740.
OrthoDBEOG7XPZG1.

Gene expression databases

GenevestigatorQ03964.

Family and domain databases

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

Other

NextBio969504.

Entry information

Entry nameYD17A_YEAST
AccessionPrimary (citable) accession number: Q03964
Secondary accession number(s): D6VSF2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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