ID   YD17A_YEAST             Reviewed;         440 AA.
AC   Q03964; D6VSF2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Transposon Ty1-DR2 Gag polyprotein;
DE   AltName: Full=Gag-p49;
DE   AltName: Full=Transposon Ty1 protein A;
DE            Short=TY1A;
DE            Short=TYA;
DE   AltName: Full=p58;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CA;
DE     AltName: Full=Gag-p45;
DE     AltName: Full=p54;
DE   Contains:
DE     RecName: Full=Gag-p4;
GN   Name=TY1A-DR2; OrderedLocusNames=YDR170W-A; ORFNames=YD9395.02;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
CC   -!- FUNCTION: Capsid protein (CA) is the structural component of the virus-
CC       like particle (VLP), forming the shell that encapsulates the
CC       retrotransposons dimeric RNA genome. The particles are assembled from
CC       trimer-clustered units and there are holes in the capsid shells that
CC       allow for the diffusion of macromolecules. CA has also nucleocapsid-
CC       like chaperone activity, promoting primer tRNA(i)-Met annealing to the
CC       multipartite primer-binding site (PBS), dimerization of Ty1 RNA and
CC       initiation of reverse transcription (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all
CC       its nucleocapsid-like chaperone activities. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Retrotransposons are mobile genetic entities that are
CC       able to replicate via an RNA intermediate and a reverse transcription
CC       step. In contrast to retroviruses, retrotransposons are non-infectious,
CC       lack an envelope and remain intracellular. Ty1 retrotransposons belong
CC       to the copia elements (pseudoviridae).
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DR   EMBL; Z46727; CAA86697.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12012.1; -; Genomic_DNA.
DR   PIR; S49765; S49765.
DR   RefSeq; NP_010455.1; NM_001184320.1.
DR   AlphaFoldDB; Q03964; -.
DR   SMR; Q03964; -.
DR   BioGRID; 32223; 10.
DR   DIP; DIP-8799N; -.
DR   IntAct; Q03964; 4.
DR   iPTMnet; Q03964; -.
DR   MaxQB; Q03964; -.
DR   PaxDb; 4932-YDR170W-A; -.
DR   PeptideAtlas; Q03964; -.
DR   GeneID; 851750; -.
DR   KEGG; sce:YDR170W-A; -.
DR   AGR; SGD:S000007227; -.
DR   SGD; S000007227; YDR170W-A.
DR   VEuPathDB; FungiDB:YDR170W-A; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_045291_1_0_1; -.
DR   InParanoid; Q03964; -.
DR   OMA; ANLHYNG; -.
DR   OrthoDB; 2040861at2759; -.
DR   PRO; PR:Q03964; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03964; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
DR   GO; GO:0003723; F:RNA binding; ISS:SGD.
DR   GO; GO:0032197; P:retrotransposition; ISS:SGD.
DR   InterPro; IPR015820; TYA.
DR   Pfam; PF01021; TYA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; RNA-binding; Transposable element.
FT   CHAIN           1..440
FT                   /note="Transposon Ty1-DR2 Gag polyprotein"
FT                   /id="PRO_0000279040"
FT   CHAIN           1..401
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279041"
FT   PEPTIDE         402..440
FT                   /note="Gag-p4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279042"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..401
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          350..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            401..402
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  49445 MW;  5E10CEE8878CD80E CRC64;
     MESQQLSQHS PISHGSACAS VTSKEVQTTQ DPLDISASKT EECEKVFTQA NSQQPTTPPS
     AAVPENHHHA SPQAAQVPLP QNGPYPQQRM MTPQQANISG WPVYGHPSLM PYPPYQMSPM
     YAPPGAQSQF TQYPQYVGTH LNTPSPESGN SFPDSSSAKS NMTSTNQHVR PPPILTSPND
     FLNWVKIYIK FLQNSNLGDI IPTATRKAVR QMTDDELTFL CHTFQLFALS QFLPTWVKDI
     LSVDYTDIMK ILSKSINKMQ SDTQEVNDIT TLANLHYNGS TPADAFEAEV TNILDRLKNN
     GIPINNKVAC QFIMRGLSGE YKFLRYARHR YIHMTVADLF SDIHSMYEEQ QESKRNKSTY
     RRSPSDEKKD SRTYTNTTKP KSITRNSQKP NNSQSRTARA HNVSTSNNFP GPDNDLIRGS
     TTEPIQLKNK HDLHLRPGTY
//