TY1A_YEASX
ID TY1A_YEASX Reviewed; 440 AA.
AC P08405; Q07155;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Transposon TyH3 Gag polyprotein;
DE AltName: Full=Gag-p49;
DE AltName: Full=Transposon Ty1-H3 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; Synonyms=GAG, TYA1;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TY1-15 ILE-12;
RP 74-THR--SER-79 AND ARG-142.
RX PubMed=2982101; DOI=10.1038/313243a0;
RA Mellor J., Fulton S.M., Dobson M.J., Wilson W., Kingsman S.M.,
RA Kingsman A.J.;
RT "A retrovirus-like strategy for expression of a fusion protein encoded by
RT yeast transposon Ty1.";
RL Nature 313:243-246(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JB84A;
RX PubMed=2837641; DOI=10.1128/mcb.8.4.1432-1442.1988;
RA Boeke J.D., Eichinger D., Castrillon D., Fink G.R.;
RT "The Saccharomyces cerevisiae genome contains functional and nonfunctional
RT copies of transposon Ty1.";
RL Mol. Cell. Biol. 8:1432-1442(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63, AND VARIANT ILE-12.
RX PubMed=6322112; DOI=10.1093/nar/12.3.1627;
RA Bowen B.A., Fulton A.M., Tuite M.F., Kingsman S.M., Kingsman A.J.;
RT "Expression of Ty-lacZ fusions in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 12:1627-1640(1984).
RN [4]
RP PROTEIN SEQUENCE OF 398-401, AND CLEAVAGE SITE.
RX PubMed=8764068; DOI=10.1128/jvi.70.8.5548-5556.1996;
RA Merkulov G.V., Swiderek K.M., Brachmann C.B., Boeke J.D.;
RT "A critical proteolytic cleavage site near the C terminus of the yeast
RT retrotransposon Ty1 Gag protein.";
RL J. Virol. 70:5548-5556(1996).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CAPSID SHELL, AND SUBUNIT.
RX PubMed=10493857; DOI=10.1006/jmbi.1999.3055;
RA Al-Khayat H.A., Bhella D., Kenney J.M., Roth J.-F., Kingsman A.J.,
RA Martin-Rendon E., Saibil H.R.;
RT "Yeast Ty retrotransposons assemble into virus-like particles whose T-
RT numbers depend on the C-terminal length of the capsid protein.";
RL J. Mol. Biol. 292:65-73(1999).
RN [6]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10766747; DOI=10.1074/jbc.m001371200;
RA Cristofari G., Ficheux D., Darlix J.-L.;
RT "The Gag-like protein of the yeast Ty1 retrotransposon contains a nucleic
RT acid chaperone domain analogous to retroviral nucleocapsid proteins.";
RL J. Biol. Chem. 275:19210-19217(2000).
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. {ECO:0000269|PubMed:10766747}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10493857}.
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. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1.;
CC Name=Transposon TyH3 Gag polyprotein;
CC IsoId=P08405-1; Sequence=Displayed;
CC Name=Transposon TyH3 Gag-Pol polyprotein;
CC IsoId=Q07163-1; Sequence=External;
CC -!- DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all
CC its nucleocapsid-like chaperone 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. Ty1 retrotransposons belong
CC to the copia elements (pseudoviridae).
CC -!- MISCELLANEOUS: [Isoform Transposon TyH3 Gag polyprotein]: Produced by
CC conventional translation.
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DR EMBL; X01736; CAA25873.1; -; Genomic_DNA.
DR EMBL; M18706; AAA66937.1; -; Genomic_DNA.
DR EMBL; X00393; CAA25112.1; -; Genomic_DNA.
DR PIR; A21856; QQBYTY.
DR PIR; A22671; A22671.
DR AlphaFoldDB; P08405; -.
DR SMR; P08405; -.
DR VEuPathDB; FungiDB:YAR010C; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR015820; TYA.
DR Pfam; PF01021; TYA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Ribosomal frameshifting; RNA-binding; Transposable element.
FT CHAIN 1..440
FT /note="Transposon TyH3 Gag polyprotein"
FT /id="PRO_0000203494"
FT CHAIN 1..401
FT /note="Capsid protein"
FT /id="PRO_0000278975"
FT PEPTIDE 402..440
FT /note="Gag-p4"
FT /id="PRO_0000278976"
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 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..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro 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 MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12441"
FT VARIANT 12
FT /note="N -> I (in Ty1-15)"
FT /evidence="ECO:0000269|PubMed:2982101,
FT ECO:0000269|PubMed:6322112"
FT VARIANT 74..79
FT /note="PASVPP -> TAQSHS (in Ty1-15)"
FT VARIANT 142
FT /note="S -> R (in Ty1-15)"
FT /evidence="ECO:0000269|PubMed:2982101"
SQ SEQUENCE 440 AA; 49010 MW; 390883DBDF8B3516 CRC64;
MESQQLSQHS PNSHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
SAVPENPHHA SPQPASVPPP 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
