YI31A_YEAST
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 25-MAY-2022, entry version 121.
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};
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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 PaxDb; Q99219; -.
DR EnsemblFungi; YIL082W_mRNA; YIL082W; YIL082W. [Q99219-1]
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:transposition, RNA-mediated; IMP:SGD.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR045358; Ty3_capsid.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15503; PTHR15503; 1.
DR Pfam; PF19259; Ty3_capsid; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; SSF57756; 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
