ID Q0US67_PHANO Unreviewed; 199 AA.
AC Q0US67;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=60S acidic ribosomal protein P1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_05397 {ECO:0000313|EMBL:EAT87788.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT87788.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445331; EAT87788.2; -; Genomic_DNA.
DR RefSeq; XP_001795803.1; XM_001795751.1.
DR AlphaFoldDB; Q0US67; -.
DR STRING; 321614.Q0US67; -.
DR EnsemblFungi; SNOT_05397; SNOT_05397; SNOG_05397.
DR GeneID; 5972678; -.
DR KEGG; pno:SNOG_05397; -.
DR VEuPathDB; FungiDB:JI435_053970; -.
DR eggNOG; KOG1762; Eukaryota.
DR HOGENOM; CLU_114656_1_0_1; -.
DR InParanoid; Q0US67; -.
DR OrthoDB; 26483at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
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 PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT REGION 154..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 199 AA; 21203 MW; 2E039808D7E114EC CRC64;
MSLRLCRQWL LQPRAYSGEV GRHRSAYRYR PGGALAALRT SRHLTTQSLA RRLRESATAI
FGSRTSHILH CETLRQTHTT IVTTNVTMST SELATSYAAL ILADDGVDIT ADKLQSLIKA
AKIEEVEPIW TTLFAKALEG KDVKDLLLNV GSGGGAASAP AAGGAGGAAA GGADAPAEEE
KKEEEKEESD DDMGFGLFD
//
