ID   YH11A_YEAST             Reviewed;         478 AA.
AC   P0C2I4; D3DLG7;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   08-NOV-2023, entry version 99.
DE   RecName: Full=Transposon Ty1-H 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-H; Synonyms=YHRCTy1-1 GAG; OrderedLocusNames=YHR214C-C;
GN   ORFNames=YHR214C-A;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   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-H Gag polyprotein;
CC         IsoId=P0C2I4-1; Sequence=Displayed;
CC       Name=Transposon Ty1-H Gag-Pol polyprotein;
CC         IsoId=O13535-1; Sequence=External;
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-H Gag polyprotein]: Produced by
CC       conventional translation.
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DR   EMBL; U00029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006934; DAA06911.1; -; Genomic_DNA.
DR   PIR; S52602; S52602.
DR   RefSeq; NP_036195.3; NM_001184437.3. [P0C2I4-1]
DR   AlphaFoldDB; P0C2I4; -.
DR   SMR; P0C2I4; -.
DR   BioGRID; 36649; 15.
DR   iPTMnet; P0C2I4; -.
DR   MaxQB; P0C2I4; -.
DR   PaxDb; 4932-YHR214C-C; -.
DR   PeptideAtlas; P0C2I4; -.
DR   GeneID; 856624; -.
DR   KEGG; sce:YHR214C-C; -.
DR   AGR; SGD:S000007421; -.
DR   SGD; S000007421; YHR214C-C.
DR   VEuPathDB; FungiDB:YHR214C-C; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_045291_1_0_1; -.
DR   InParanoid; P0C2I4; -.
DR   OrthoDB; 2039326at2759; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P0C2I4; 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; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Ribosomal frameshifting; RNA-binding;
KW   Transposable element.
FT   CHAIN           1..478
FT                   /note="Transposon Ty1-H Gag polyprotein"
FT                   /id="PRO_0000279079"
FT   CHAIN           1..439
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279080"
FT   PEPTIDE         440..478
FT                   /note="Gag-p4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279081"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..439
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          390..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..67
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        398..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            439..440
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  53325 MW;  2A0E36FEFE4B66B9 CRC64;
     MESQQLSNYP HISHGSACAS VTSKEVHTNQ DPLDVSASKI QEYDKASTKA NSQQTTTPAS
     SAVPENLHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM
     YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND
     FPNWVKTYIK FLQNSNLGGI IPTVNGKPVP PMLTSPNDFP NWVKTYIKFL QNSNLGGIIP
     TVNGKPVRQI TDDELTFLYN TFQIFAPSQF LPTWVKDILS VDYTDIMKIL SKSIEKMQSD
     TQEANDIVTL ANLQYNGSTP ADAFETKVTN IIDRLNNNGI HINNKVACQL IMRGLSGEYK
     FLRYTRHRHL NMTVAELFLD IHAIYEEQQG SRNSKPNYRR NPSDEKNDSR SYTNTTKPKV
     IARNPQKTNN SKSKTARAHN VSTSNNSPST DNDSISKSTT EPIQLNNKHD LHLRPETY
//