ID   YI31A_YEAST             Reviewed;         290 AA.
AC   Q99219;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 127.
DE   RecName: Full=Transposon Ty3-I Gag polyprotein;
DE   AltName: Full=Gag3;
DE   AltName: Full=Transposon Ty3-2 protein A;
DE            Short=TY3A;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CA;
DE     AltName: Full=p24;
DE   Contains:
DE     RecName: Full=Spacer peptide p3;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p9;
DE              Short=NC;
DE     AltName: Full=p7;
GN   Name=TY3A-I; Synonyms=YILWTy3-1 GAG; OrderedLocusNames=YIL082W;
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 [GENOMIC DNA].
RX   PubMed=2854194; DOI=10.1128/mcb.8.12.5245-5256.1988;
RA   Hansen L.J., Chalker D.L., Sandmeyer S.B.;
RT   "Ty3, a yeast retrotransposon associated with tRNA genes, has homology to
RT   animal retroviruses.";
RL   Mol. Cell. Biol. 8:5245-5256(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
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   [6]
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.
CC   -!- FUNCTION: Nucleocapsid protein p9 (NC) forms the nucleocore that coats
CC       the retro-elements dimeric RNA. Binds these RNAs through its zinc
CC       fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the
CC       multipartite primer-binding site (PBS), dimerization of Ty3 RNA and
CC       initiation of reverse transcription. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC         Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal
CC         frameshift.;
CC       Name=Transposon Ty3-I Gag polyprotein;
CC         IsoId=Q99219-1; Sequence=Displayed;
CC       Name=Transposon Ty3-I Gag-Pol polyprotein;
CC         IsoId=Q7LHG5-1; Sequence=External;
CC   -!- DOMAIN: The N-terminal domain of NC, but not its zinc finger, is
CC       required for nucleoprotein complex formation and its chaperone
CC       activities.
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. Ty3 retrotransposons belong
CC       to the gypsy-like elements (metaviridae).
CC   -!- MISCELLANEOUS: [Isoform Transposon Ty3-I Gag polyprotein]: Produced by
CC       conventional translation.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M23367; AAA35183.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z46728; CAA86712.1; -; Genomic_DNA.
DR   EMBL; AY557875; AAS56201.1; -; Genomic_DNA.
DR   EMBL; BK006942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S41555; S41555.
DR   AlphaFoldDB; Q99219; -.
DR   SMR; Q99219; -.
DR   DIP; DIP-8996N; -.
DR   IntAct; Q99219; 1.
DR   MINT; Q99219; -.
DR   STRING; 4932.YIL082W; -.
DR   PaxDb; 4932-YIL082W; -.
DR   PeptideAtlas; Q99219; -.
DR   EnsemblFungi; YIL082W_mRNA; YIL082W; YIL082W. [Q99219-1]
DR   AGR; SGD:S000001344; -.
DR   SGD; S000001344; YIL082W.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_966938_0_0_1; -.
DR   InParanoid; Q99219; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; Q99219; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000943; C:retrotransposon nucleocapsid; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032197; P:retrotransposition; IMP:SGD.
DR   InterPro; IPR045358; Ty3_capsid.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF19259; Ty3_capsid; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Metal-binding; Reference proteome;
KW   Ribosomal frameshifting; Transposable element; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q12173"
FT   CHAIN           2..290
FT                   /note="Transposon Ty3-I Gag polyprotein"
FT                   /id="PRO_0000279376"
FT   CHAIN           2..207
FT                   /note="Capsid protein"
FT                   /id="PRO_0000279377"
FT   PEPTIDE         208..233
FT                   /note="Spacer peptide p3"
FT                   /id="PRO_0000279378"
FT   CHAIN           234..290
FT                   /note="Nucleocapsid protein p9"
FT                   /id="PRO_0000279379"
FT   ZN_FING         265..282
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   SITE            207..208
FT                   /note="Cleavage; by Ty3 protease"
FT   SITE            233..234
FT                   /note="Cleavage; by Ty3 protease"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12173"
SQ   SEQUENCE   290 AA;  34100 MW;  5113F9717ADD196A CRC64;
     MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML NMSMISWPND
     ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL YQHFYKPPDI NKIFNAITQL
     SEAKLGIERL NQRFRKIWDR MPPDFMTEKA AIMTYTRLLT KETYNIVRMH KPETLKDAME
     EAYQTTALTE RFFPGFELDA DGDTIIGATT HLQEEYDSDY DSEDNLTQNR YVHTVRTRRS
     YNKPMSNHRN RRNNNASREE CIKNRLCFYC KKEGHRLNEC RARKASSNRS
//