ID G0U5Y1_TRYVY Unreviewed; 121 AA.
AC G0U5Y1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative 60S acidic ribosomal protein P2 {ECO:0000313|EMBL:CCC51282.1};
GN ORFNames=TVY486_1003340 {ECO:0000313|EMBL:CCC51281.1}, TVY486_1003350
GN {ECO:0000313|EMBL:CCC51282.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCC51282.1};
RN [1] {ECO:0000313|EMBL:CCC51282.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y486 {ECO:0000313|EMBL:CCC51282.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis. {ECO:0000256|ARBA:ARBA00003362}.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00011266}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000256|ARBA:ARBA00005436}.
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DR EMBL; HE573026; CCC51281.1; -; Genomic_DNA.
DR EMBL; HE573026; CCC51282.1; -; Genomic_DNA.
DR AlphaFoldDB; G0U5Y1; -.
DR VEuPathDB; TriTrypDB:TvY486_1003340; -.
DR VEuPathDB; TriTrypDB:TvY486_1003350; -.
DR OrthoDB; 26483at2759; -.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR CDD; cd05831; Ribosomal_P1; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_P1/P2.
DR InterPro; IPR001859; Ribosomal_P1/P2_euk.
DR PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF41; ACIDIC RIBOSOMAL PROTEIN P2, PUTATIVE-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR PRINTS; PR00456; RIBOSOMALP2.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000313|EMBL:CCC51282.1}.
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 121 AA; 11795 MW; 8CD0095A0706FCAF CRC64;
MAKAINPTDT LACTYAALML SDAGAPITAE NISAACNAAG LQVRSTLPIL FARFLEKKPI
ETLLAAAAAV APQAGADVAP AASAASGGAG AAAGGAAAGA GKESKKVEEE EDDDMGFGLF
D
//
