Q03964 (YD17A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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).

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	RNA-binding
Technical term	Complete proteome Reference proteome Transposable element
Gene Ontology (GO)
Biological_process	transposition, RNA-mediated Inferred from sequence or structural similarity PubMed 9582191. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD retrotransposon nucleocapsid Inferred from sequence or structural similarity PubMed 9582191. Source: SGD
Molecular_function	RNA binding Inferred from sequence or structural similarity PubMed 9582191. 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-DR2 Gag polyprotein		PRO_0000279040
	Chain	1 – 401	401	Capsid protein By similarity		PRO_0000279041
	Peptide	402 – 440	39	Gag-p4 By similarity		PRO_0000279042
Regions
	Region	299 – 401	103	RNA-binding By similarity
Sites
	Site	401 – 402	2	Cleavage; by Ty1 protease By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03964 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5E10CEE8878CD80E	FASTA	440	49,445
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	S49765.
RefSeq	NP_010455.1. NM_001184320.1.
3D structure databases
ProteinModelPortal	Q03964.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8799N.
IntAct	Q03964. 4 interactions.
MINT	MINT-680391.
STRING	4932.YDR170W-A.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR170W-A; YDR170W-A; YDR170W-A.
GeneID	851750.
KEGG	sce:YDR170W-A.
Organism-specific databases
CYGD	YDR170w-a.
SGD	S000007227. YDR170W-A.
Phylogenomic databases
GeneTree	ENSGT00700000104791.
HOGENOM	HOG000000740.
OrthoDB	EOG4V1BB5.
Gene expression databases
Genevestigator	Q03964.
Family and domain databases
InterPro	IPR015820. Retrotransposon_Ty1A_N. [Graphical view]
Pfam	PF01021. TYA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969504.

Entry information

Entry name

YD17A_YEAST

Accession

Primary (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 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program