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Transposon Ty1-DR4 Gag polyprotein (Gag-p49) (Transposon Ty1 protein A) (TY1A) (TYA) (p58) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Gag-p4]

 YD13A_YEAST             Reviewed;         440 AA.
O74302; D6VSP5;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-FEB-2018, entry version 96.
RecName: Full=Transposon Ty1-DR4 Gag polyprotein;
AltName: Full=Gag-p49;
AltName: Full=Transposon Ty1 protein A;
Short=TY1A;
Short=TYA;
AltName: Full=p58;
Contains:
RecName: Full=Capsid protein;
Short=CA;
AltName: Full=Gag-p45;
AltName: Full=p54;
Contains:
RecName: Full=Gag-p4;
Name=TY1A-DR4; Synonyms=YDRCTy1-3 GAG; OrderedLocusNames=YDR261C-C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NOMENCLATURE.
PubMed=9582191;
Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.;
"Transposable elements and genome organization: a comprehensive survey
of retrotransposons revealed by the complete Saccharomyces cerevisiae
genome sequence.";
Genome Res. 8:464-478(1998).
[4]
INDUCTION.
PubMed=11884596; DOI=10.1128/MCB.22.7.2078-2088.2002;
Morillon A., Benard L., Springer M., Lesage P.;
"Differential effects of chromatin and Gcn4 on the 50-fold range of
expression among individual yeast Ty1 retrotransposons.";
Mol. Cell. Biol. 22:2078-2088(2002).
[5]
REVIEW.
PubMed=16093660; DOI=10.1159/000084940;
Lesage P., Todeschini A.L.;
"Happy together: the life and times of Ty retrotransposons and their
hosts.";
Cytogenet. Genome Res. 110:70-90(2005).
-!- 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). {ECO:0000250}.
-!- SUBUNIT: Homotrimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- 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). {ECO:0000250};
Name=Transposon Ty1-DR4 Gag polyprotein;
IsoId=O74302-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Transposon Ty1-DR4 Gag-Pol polyprotein;
IsoId=Q07793-1; Sequence=External;
Note=Produced by +1 ribosomal frameshifting between codon
Leu-435 and Gly-436 of the YDR261C-C ORF.;
-!- INDUCTION: Ty1-DR4 is a highly expressed element. Induced under
amino acid starvation conditions by GCN4.
{ECO:0000269|PubMed:11884596}.
-!- DOMAIN: The C-terminal RNA-binding region of CA is sufficient for
all its nucleocapsid-like chaperone activities. {ECO:0000250}.
-!- 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).
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EMBL; Z74387; CAA98915.1; -; Genomic_DNA.
EMBL; BK006938; DAA12105.1; -; Genomic_DNA.
PIR; S70228; S70228.
RefSeq; NP_058149.1; NM_001184420.1. [O74302-1]
SMR; O74302; -.
BioGrid; 32316; 3.
IntAct; O74302; 3.
MINT; O74302; -.
STRING; 4932.YDR261C-C; -.
PaxDb; O74302; -.
PRIDE; O74302; -.
EnsemblFungi; YDR261C-C; YDR261C-C; YDR261C-C. [O74302-1]
GeneID; 851853; -.
KEGG; sce:YDR261C-C; -.
EuPathDB; FungiDB:YDR261C-C; -.
SGD; S000007394; YDR261C-C.
GeneTree; ENSGT00910000144299; -.
HOGENOM; HOG000000740; -.
InParanoid; O74302; -.
OrthoDB; EOG092C24YV; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
GO; GO:0003723; F:RNA binding; ISS:SGD.
GO; GO:0032197; P:transposition, RNA-mediated; ISS:SGD.
InterPro; IPR015820; Retrotransposon_Ty1A_N.
Pfam; PF01021; TYA; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
Ribosomal frameshifting; RNA-binding; Transposable element.
CHAIN 1 440 Transposon Ty1-DR4 Gag polyprotein.
/FTId=PRO_0000279022.
CHAIN 1 401 Capsid protein. {ECO:0000250}.
/FTId=PRO_0000279023.
PEPTIDE 402 440 Gag-p4. {ECO:0000250}.
/FTId=PRO_0000279024.
REGION 299 401 RNA-binding. {ECO:0000250}.
COMPBIAS 64 146 Pro-rich.
SITE 401 402 Cleavage; by Ty1 protease. {ECO:0000250}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:Q12441}.
SEQUENCE 440 AA; 49009 MW; F685C7C98B6DEE8D CRC64;
MESQQLSQHS PISHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
SAVPENPHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM
YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND
FPNWVKTYIK FLQNSNLGGI IPTVNGKPVR QITDDELTFL YNTFQIFAPS QFLPTWVKDI
LSVDYTDIMK ILSKSIEKMQ SDTQEANDIV TLANLQYNGS TPADAFETKV TNIIDRLNNN
GIHINNKVAC QLIMRGLSGE YKFLRYTRHR HLNMTVAELF LDIHAIYEEQ QGSRNSKPNY
RRNPSDEKND SRSYTNTTKP KVIARNPQKT NNSKSKTARA HNVSTSNNSP STDNDSISKS
TTEPIQLNNK HDLHLRPETY


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