YG31A_YEAST
ID YG31A_YEAST Reviewed; 290 AA.
AC Q12173; D6VUP2; Q07096; Q9P311;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Transposon Ty3-G Gag polyprotein;
DE AltName: Full=Gag3;
DE AltName: Full=Transposon Ty3-1 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 Short=NCp9;
DE AltName: Full=p7;
GN Name=TY3A-G; Synonyms=YGRWTy3-1 GAG; OrderedLocusNames=YGR109W-A;
GN ORFNames=G5982;
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], AND FUNCTION.
RC STRAIN=AB950;
RX PubMed=2159534; DOI=10.1128/jvi.64.6.2599-2607.1990;
RA Hansen L.J., Sandmeyer S.B.;
RT "Characterization of a transpositionally active Ty3 element and
RT identification of the Ty3 integrase protein.";
RL J. Virol. 64:2599-2607(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=2447089; DOI=10.1016/s0021-9258(19)57319-7;
RA Clark D.J., Bilanchone V.W., Haywood L.J., Dildine S.L., Sandmeyer S.B.;
RT "A yeast sigma composite element, TY3, has properties of a
RT retrotransposon.";
RL J. Biol. Chem. 263:1413-1423(1988).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=1371165; DOI=10.1128/jvi.66.3.1414-1424.1992;
RA Hansen L.J., Chalker D.L., Orlinsky K.J., Sandmeyer S.B.;
RT "Ty3 GAG3 and POL3 genes encode the components of intracellular
RT particles.";
RL J. Virol. 66:1414-1424(1992).
RN [8]
RP PROTEOLYTIC PROCESSING, AND CLEAVAGE SITES.
RX PubMed=7677953; DOI=10.1128/jvi.67.1.19-28.1993;
RA Kirchner J., Sandmeyer S.B.;
RT "Proteolytic processing of Ty3 proteins is required for transposition.";
RL J. Virol. 67:19-28(1993).
RN [9]
RP FUNCTION OF NUCLEOCAPSID, AND MUTAGENESIS OF CYS-267 AND HIS-275.
RX PubMed=7515969; DOI=10.1128/jvi.68.7.4152-4166.1994;
RA Orlinsky K.J., Sandmeyer S.B.;
RT "The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3
RT polyproteins.";
RL J. Virol. 68:4152-4166(1994).
RN [10]
RP FUNCTION.
RX PubMed=9707446; DOI=10.1093/emboj/17.16.4873;
RA Gabus C., Ficheux D., Rau M., Keith G., Sandmeyer S.B., Darlix J.-L.;
RT "The yeast Ty3 retrotransposon contains a 5'-3' bipartite primer-binding
RT site and encodes nucleocapsid protein NCp9 functionally homologous to HIV-1
RT NCp7.";
RL EMBO J. 17:4873-4880(1998).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=10593967; DOI=10.1074/jbc.274.51.36643;
RA Cristofari G., Gabus C., Ficheux D., Bona M., Le Grice S.F.J.,
RA Darlix J.-L.;
RT "Characterization of active reverse transcriptase and nucleoprotein
RT complexes of the yeast retrotransposon Ty3 in vitro.";
RL J. Biol. Chem. 274:36643-36648(1999).
RN [13]
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 [14]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, CLEAVAGE SITE
RP GLY-207-208-ALA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15956549; DOI=10.1128/jvi.79.13.8032-8045.2005;
RA Kuznetsov Y.G., Zhang M., Menees T.M., McPherson A., Sandmeyer S.B.;
RT "Investigation by atomic force microscopy of the structure of Ty3
RT retrotransposon particles.";
RL J. Virol. 79:8032-8045(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 ECO:0000269|PubMed:10593967, ECO:0000269|PubMed:2159534,
CC ECO:0000269|PubMed:7515969, ECO:0000269|PubMed:9707446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1371165}.
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-G Gag polyprotein;
CC IsoId=Q12173-1; Sequence=Displayed;
CC Name=Transposon Ty3-G Gag-Pol polyprotein;
CC IsoId=Q99315-1; 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-G Gag polyprotein]: Produced by
CC conventional translation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98434.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M34549; AAA98434.2; ALT_INIT; Genomic_DNA.
DR EMBL; Z72894; CAA97114.1; -; Genomic_DNA.
DR EMBL; Z72895; CAA97116.1; -; Genomic_DNA.
DR EMBL; AY557824; AAS56150.1; -; Genomic_DNA.
DR EMBL; M18353; AAA66936.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08203.1; -; Genomic_DNA.
DR PIR; S22875; S22875.
DR PIR; S69841; S69841.
DR RefSeq; NP_058162.3; NM_001184380.3. [Q12173-1]
DR AlphaFoldDB; Q12173; -.
DR SMR; Q12173; -.
DR BioGRID; 33355; 4.
DR STRING; 4932.YGR109W-A; -.
DR iPTMnet; Q12173; -.
DR PaxDb; Q12173; -.
DR GeneID; 853005; -.
DR KEGG; sce:YGR109W-A; -.
DR SGD; S000007346; YGR109W-A.
DR VEuPathDB; FungiDB:YGR109W-A; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_966938_0_0_1; -.
DR InParanoid; Q12173; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q12173; 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; IPR045358; Ty3_capsid.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19259; Ty3_capsid; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
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:0000269|PubMed:15956549"
FT CHAIN 2..290
FT /note="Transposon Ty3-G Gag polyprotein"
FT /id="PRO_5000143279"
FT CHAIN 2..207
FT /note="Capsid protein"
FT /id="PRO_0000279365"
FT PEPTIDE 208..233
FT /note="Spacer peptide p3"
FT /id="PRO_0000279366"
FT CHAIN 234..290
FT /note="Nucleocapsid protein p9"
FT /id="PRO_5000143280"
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:0000269|PubMed:15956549"
FT MUTAGEN 267
FT /note="C->S: Reduces level of VLP formation and
FT maturation."
FT /evidence="ECO:0000269|PubMed:7515969"
FT MUTAGEN 275
FT /note="H->Q: Reduces level of VLP formation and
FT maturation."
FT /evidence="ECO:0000269|PubMed:7515969"
SQ SEQUENCE 290 AA; 34027 MW; 4D63E26BDE78197F CRC64;
MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML NMSMISWPND
ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL YQHFYKPPDI NKIFNAITQL
SEAKLGIERL NQRFRKIWDR MPPDFMTEKA AIMTYTRLLT KETYNIVRMH KPETLKDAME
EAYQTTALTE RFFPGFELDA DGDTIIGATT HLQEEYDSDY DSEDNLTQNG YVHTVRTRRS
YNKPMSNHRN RRNNNPSREE CIKNRLCFYC KKEGHRLNEC RARKASSNRS
