ID   YP12A_YEAST             Reviewed;         440 AA.
AC   P0CX58; D6VPM2; O13528;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Transposon Ty1-PR1 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-PR1; Synonyms=YPRCTy1-2 GAG; OrderedLocusNames=YPR137C-A;
GN   ORFNames=P9659.6d;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=9582191; DOI=10.1101/gr.8.5.464;
RA   Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.;
RT   "Transposable elements and genome organization: a comprehensive survey of
RT   retrotransposons revealed by the complete Saccharomyces cerevisiae genome
RT   sequence.";
RL   Genome Res. 8:464-478(1998).
RN   [4]
RP   INDUCTION.
RX   PubMed=11884596; DOI=10.1128/mcb.22.7.2078-2088.2002;
RA   Morillon A., Benard L., Springer M., Lesage P.;
RT   "Differential effects of chromatin and Gcn4 on the 50-fold range of
RT   expression among individual yeast Ty1 retrotransposons.";
RL   Mol. Cell. Biol. 22:2078-2088(2002).
RN   [5]
RP   REVIEW.
RX   PubMed=16093660; DOI=10.1159/000084940;
RA   Lesage P., Todeschini A.L.;
RT   "Happy together: the life and times of Ty retrotransposons and their
RT   hosts.";
RL   Cytogenet. Genome Res. 110:70-90(2005).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC         Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal
CC         frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By
CC         similarity). {ECO:0000250};
CC       Name=Transposon Ty1-PR1 Gag polyprotein;
CC         IsoId=P0CX58-1; Sequence=Displayed;
CC       Name=Transposon Ty1-PR1 Gag-Pol polyprotein;
CC         IsoId=P0C2I9-1; Sequence=External;
CC   -!- INDUCTION: Ty1-PR1 is a highly expressed element. Induced under amino
CC       acid starvation conditions by GCN4. {ECO:0000269|PubMed:11884596}.
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).
CC   -!- MISCELLANEOUS: [Isoform Transposon Ty1-PR1 Gag polyprotein]: Produced
CC       by conventional translation.
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DR   EMBL; U40829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006949; DAA11551.1; -; Genomic_DNA.
DR   PIR; S40909; S40909.
DR   RefSeq; NP_009407.1; NM_001178214.1. [P0CX58-1]
DR   RefSeq; NP_058192.1; NM_001184393.1. [P0CX58-1]
DR   AlphaFoldDB; P0CX58; -.
DR   SMR; P0CX58; -.
DR   BioGRID; 31796; 24.
DR   BioGRID; 36305; 20.
DR   IntAct; P0CX58; 1.
DR   MINT; P0CX58; -.
DR   iPTMnet; P0CX58; -.
DR   MaxQB; P0CX58; -.
DR   GeneID; 851269; -.
DR   GeneID; 856258; -.
DR   KEGG; sce:YAR010C; -.
DR   KEGG; sce:YPR137C-A; -.
DR   AGR; SGD:S000007359; -.
DR   SGD; S000007359; YPR137C-A.
DR   VEuPathDB; FungiDB:YAR010C; -.
DR   VEuPathDB; FungiDB:YPR137C-A; -.
DR   HOGENOM; CLU_045291_1_0_1; -.
DR   InParanoid; P0CX58; -.
DR   OrthoDB; 2039326at2759; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P0CX58; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Ribosomal frameshifting;
KW   RNA-binding; Transposable element.
FT   CHAIN           1..440
FT                   /note="Transposon Ty1-PR1 Gag polyprotein"
FT                   /id="PRO_0000409776"
FT   CHAIN           1..401
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409777"
FT   PEPTIDE         402..440
FT                   /note="Gag-p4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409778"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..401
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          352..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            401..402
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12441"
SQ   SEQUENCE   440 AA;  49072 MW;  DCE9E5C434D51201 CRC64;
     MESQQLSQHS PISHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
     SAVPENPHHA SPQTAQSHSP 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
//