YO22A_YEAST
ID YO22A_YEAST Reviewed; 438 AA.
AC Q12293; D6W339;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Transposon Ty2-OR2 Gag polyprotein;
DE Short=TY2A;
DE Short=TYA;
DE Short=Transposon Ty2 protein A;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CA;
DE Contains:
DE RecName: Full=Gag-p4;
GN Name=TY2A-OR2; Synonyms=YORWTy2-2 GAG; OrderedLocusNames=YOR343W-A;
GN ORFNames=O6301;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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-OR2 Gag polyprotein;
CC IsoId=Q12293-1; Sequence=Displayed;
CC Name=Transposon Ty2-OR2 Gag-Pol polyprotein;
CC IsoId=Q12501-1; 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-OR2 Gag polyprotein]: Produced
CC by conventional translation.
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; Z75251; CAA99669.1; -; Genomic_DNA.
DR EMBL; Z75252; CAA99672.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11105.1; -; Genomic_DNA.
DR PIR; S70232; S70232.
DR RefSeq; NP_620390.1; NM_001184389.1. [Q12293-1]
DR AlphaFoldDB; Q12293; -.
DR BioGRID; 34726; 1.
DR STRING; 4932.YOR343W-A; -.
DR MEROPS; A11.003; -.
DR PaxDb; Q12293; -.
DR GeneID; 854522; -.
DR KEGG; sce:YOR343W-A; -.
DR SGD; S000007355; YOR343W-A.
DR VEuPathDB; FungiDB:YOR343W-A; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_045291_1_0_1; -.
DR InParanoid; Q12293; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12293; 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; RNA-binding;
KW Transposable element.
FT CHAIN 1..438
FT /note="Transposon Ty2-OR2 Gag polyprotein"
FT /id="PRO_0000279353"
FT CHAIN 1..397
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279354"
FT PEPTIDE 398..438
FT /note="Gag-p4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279355"
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 21..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"
SQ SEQUENCE 438 AA; 49867 MW; 020AB4FAC4B32500 CRC64;
MESQQLHQNP HCPHGSAYAS VTSKEVPSNQ DPLAVSASNL PEFDRDSTKV NSQEETTPGT
SAVPENHHHV SPQPASVPPP QNGQYQQHGM MTPNKAMASN WAHYQQPSMM TCSHYQTSPA
YYQPDPHYPL PQYIPPLSTS SPDPIDSQDQ HSEVPQAKTK VRNNVLPPHP HTSEENFSTW
VKFYIRFLKN SNLGDIIPND QGEIKRQMTY EEHAYIYNTF QAFAPFHLLP TWVKQILEIN
YSDILTVLCK SVSKMQTNNQ ELKDWIALAN LEYNGSTSAD TFEITVSTII QRLKENNINV
SDRLACQLIL KGLSGDFKYL RNQYRTKTNM KLSQLFAEIQ LIYDENKIMN LNKPSQYKQH
SEYKNVSRTS PNTTNTKVTT RNYHRTNSSK PRAAKAHNIA TSSKFSRVNN DHINESTVSS
QYLSDDNELS LRPATERI
