YC21A_YEAST
ID YC21A_YEAST Reviewed; 438 AA.
AC P25383; D6VQZ5; Q07125;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transposon Ty2-C Gag polyprotein;
DE AltName: Full=Transposon Ty2 protein A;
DE Short=TY2A;
DE Short=TYA;
DE AltName: Full=Ty1-17 protein A;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CA;
DE Contains:
DE RecName: Full=Gag-p4;
GN Name=TY2A-C; Synonyms=YCLWTy2-1 GAG; OrderedLocusNames=YCL020W;
GN ORFNames=YCL20W;
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=3010239; DOI=10.1093/nar/14.8.3475;
RA Warmington J.R., Anwar R., Newlon C.S., Waring R.B., Davies R.W.,
RA Indge K.J., Oliver S.G.;
RT "A 'hot-spot' for Ty transposition on the left arm of yeast chromosome
RT III.";
RL Nucleic Acids Res. 14:3475-3485(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2997719; DOI=10.1093/nar/13.18.6679;
RA Warmington J.R., Waring R.B., Newlon C.S., Indge K.J., Oliver S.G.;
RT "Nucleotide sequence characterization of Ty 1-17, a class II transposon
RT from yeast.";
RL Nucleic Acids Res. 13:6679-6693(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MD 40-4C;
RX PubMed=2989787; DOI=10.1093/nar/13.11.4097;
RA Fulton A.M., Mellor J., Dobson M.J., Chester J., Warmington J.R.,
RA Indge K.J., Oliver S.G., de la Paz P., Wilson W., Kingsman A.J.,
RA Kingsman S.M.;
RT "Variants within the yeast Ty sequence family encode a class of
RT structurally conserved proteins.";
RL Nucleic Acids Res. 13:4097-4112(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [5]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
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 [8]
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 [9]
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 Ty2 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.;
CC Name=Transposon Ty2-C Gag polyprotein;
CC IsoId=P25383-1; Sequence=Displayed;
CC Name=Transposon Ty2-C Gag-Pol polyprotein;
CC IsoId=P25384-1; 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. Ty2 retrotransposons belong
CC to the copia elements (pseudoviridae).
CC -!- MISCELLANEOUS: [Isoform Transposon Ty2-C Gag polyprotein]: Produced by
CC conventional translation.
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DR EMBL; X03840; CAA27457.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42364.2; -; Genomic_DNA.
DR EMBL; X02546; CAA26398.1; -; Genomic_DNA.
DR EMBL; X00394; CAA25113.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07464.1; -; Genomic_DNA.
DR PIR; S19347; S19347.
DR RefSeq; NP_009910.2; NM_001178667.1. [P25383-1]
DR AlphaFoldDB; P25383; -.
DR BioGRID; 30963; 7.
DR DIP; DIP-7334N; -.
DR IntAct; P25383; 2.
DR MINT; P25383; -.
DR STRING; 4932.YCL020W; -.
DR PaxDb; P25383; -.
DR PRIDE; P25383; -.
DR GeneID; 850339; -.
DR KEGG; sce:YCL020W; -.
DR SGD; S000000525; YCL020W.
DR VEuPathDB; FungiDB:YCL020W; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_045291_1_0_1; -.
DR InParanoid; P25383; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25383; 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 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Ribosomal frameshifting;
KW Transposable element.
FT CHAIN 1..438
FT /note="Transposon Ty2-C Gag polyprotein"
FT /id="PRO_0000203495"
FT CHAIN 1..397
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279282"
FT PEPTIDE 398..438
FT /note="Gag-p4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279283"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..397
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 365..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..438
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 SITE 397..398
FT /note="Cleavage; by Ty2 protease"
FT /evidence="ECO:0000250"
FT CONFLICT 174
FT /note="E -> D (in Ref. 1 and 2; CAA27457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 49841 MW; D92E6A7BDA32A5B4 CRC64;
MESQQLHQNP RSLHGSAYAS VTSKEVPSNQ DPLAVSASNL PEFDRDSTKV NSQQETTPGT
SAVPENHHHV SPQPASVPPP QNGQYQQHGM MTPNKAMASN WAHYQQPSMM TCSHYQTSPA
YYQPDPHYPL PQYIPPLSTS SPDPIDSQNQ HSEVPQAETK VRNNVLPPHT LTSEENFSTW
VKFYIRFLKN SNLGDIIPND QGEIKRQMTY EEHAYIYNTF QAFAPFHLLP TWVKQILEIN
YADILTVLCK SVSKMQTNNQ ELKDWIALAN LEYDGSTSAD TFEITVSTII QRLKENNINV
SDRLACQLIL KGLSGDFKYL RNQYRTKTNM KLSQLFAEIQ LIYDENKIMN LNKPSQYKQH
SEYKNVSRTS PNTTNTKVTT RNYQRTNSSK PRAAKAHNIA TSSKFSRVNN DHINESTVSS
QYLSDDNELS LRPATERI
