YM13A_YEAST
ID YM13A_YEAST Reviewed; 440 AA.
AC Q04215; D6VZM1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Transposon Ty1-MR1 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-MR1; Synonyms=YMRCTy1-3 GAG; OrderedLocusNames=YMR046C;
GN ORFNames=YM9532.11C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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-MR1 Gag polyprotein;
CC IsoId=Q04215-1; Sequence=Displayed;
CC Name=Transposon Ty1-MR1 Gag-Pol polyprotein;
CC IsoId=Q04214-1; Sequence=External;
CC -!- INDUCTION: Ty1-MR1 is a weakly 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-MR1 Gag polyprotein]: Produced
CC by conventional translation.
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DR EMBL; Z48502; CAA88412.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09945.1; -; Genomic_DNA.
DR PIR; S52895; S52895.
DR RefSeq; NP_013760.1; NM_001182543.1. [Q04215-1]
DR AlphaFoldDB; Q04215; -.
DR SMR; Q04215; -.
DR BioGRID; 35219; 8.
DR IntAct; Q04215; 2.
DR STRING; 4932.YMR046C; -.
DR MaxQB; Q04215; -.
DR PaxDb; Q04215; -.
DR GeneID; 855063; -.
DR KEGG; sce:YMR046C; -.
DR SGD; S000004649; YMR046C.
DR VEuPathDB; FungiDB:YMR046C; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_045291_1_0_1; -.
DR InParanoid; Q04215; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04215; 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:transposition, RNA-mediated; ISS:SGD.
DR InterPro; IPR015820; TYA.
DR Pfam; PF01021; TYA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Ribosomal frameshifting; RNA-binding;
KW Transposable element.
FT CHAIN 1..440
FT /note="Transposon Ty1-MR1 Gag polyprotein"
FT /id="PRO_0000203499"
FT CHAIN 1..401
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279131"
FT PEPTIDE 402..440
FT /note="Gag-p4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279132"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..401
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 350..424
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 137..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..424
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"
SQ SEQUENCE 440 AA; 49274 MW; 6948648D0FEE321E CRC64;
MESQQLSQHS PISHGSACAS VTSKEVQTTQ DPLDISASKT EECEKVSTQA NSQQPTTPLS
SAVPENHHHA SPQAAQVPLP QNGPYPQQRM MNTQQANISG WPVYGHPSLM PYPPYQMSPM
YAPPGAQSQF TQYPQYVGTH LNTPSPESGN SFPDSSSAKS NMTSTNQHVR PPPILTSPND
FLNWVKIYIK FLQNSNLGDI IPTATRKAVR QMTDDELTFL CHTFQLFAPS QFLPPWVKDI
LSVDYTDIMK ILSKSINKMQ SDTQEVNDIT TLATLHYNGS TPADAFEAEV TNILDRLNNN
GIPINNKVAC QFIMRGLSGE YKFLRYARHR CIHMTVADLF SDIHSMYEEQ QESKRNKSTH
RRSPSDEKKD SRTYTNTTKP KSITRNSQKP NNSQSRTARA HNVSTFNNSP GPDNDLIRGS
TTEPIQLKNT HDLHLRPGTY
