YA11A_YEAST
ID YA11A_YEAST Reviewed; 440 AA.
AC P0CX57; D6VPM2; O13528;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Transposon Ty1-A 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-A; Synonyms=YARCTy1-1 GAG; OrderedLocusNames=YAR010C;
GN ORFNames=P9659.6d;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
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 [4]
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 [5]
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 [6]
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 Ty1 RNA and
CC initiation of reverse transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Ty1-A 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 -!- CAUTION: Transposon Ty1-A (YARCTy1-1) contains a frameshift at position
CC 610, which disrupts the ORF coding for protein TY1B. {ECO:0000305}.
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; L22015; AAC04966.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06992.1; -; Genomic_DNA.
DR PIR; S40909; S40909.
DR RefSeq; NP_009407.1; NM_001178214.1.
DR RefSeq; NP_058192.1; NM_001184393.1.
DR AlphaFoldDB; P0CX57; -.
DR SMR; P0CX57; -.
DR BioGRID; 31796; 22.
DR BioGRID; 36305; 19.
DR STRING; 4932.YAR010C; -.
DR iPTMnet; P0CX57; -.
DR PaxDb; P0CX57; -.
DR GeneID; 851269; -.
DR GeneID; 856258; -.
DR KEGG; sce:YAR010C; -.
DR KEGG; sce:YPR137C-A; -.
DR SGD; S000000068; YAR010C.
DR VEuPathDB; FungiDB:YAR010C; -.
DR VEuPathDB; FungiDB:YPR137C-A; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_045291_1_0_1; -.
DR InParanoid; P0CX57; -.
DR PRO; PR:P0CX57; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P0CX57; 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 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding;
KW Transposable element.
FT CHAIN 1..440
FT /note="Transposon Ty1-A Gag polyprotein"
FT /id="PRO_0000278982"
FT CHAIN 1..401
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000278983"
FT PEPTIDE 402..440
FT /note="Gag-p4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000278984"
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 /evidence="ECO:0000250"
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..93
FT /note="Polar 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 /evidence="ECO:0000250"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12441"
SQ SEQUENCE 440 AA; 49072 MW; DCE9E5C434D51201 CRC64;
MESQQLSQHS PISHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
SAVPENPHHA SPQTAQSHSP 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
