ID A0A420XY36_9PEZI Unreviewed; 315 AA.
AC A0A420XY36;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN Name=RPP0 {ECO:0000313|EMBL:RKU40565.1};
GN ORFNames=DL546_000746 {ECO:0000313|EMBL:RKU40565.1};
OS Coniochaeta pulveracea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU40565.1, ECO:0000313|Proteomes:UP000275385};
RN [1] {ECO:0000313|EMBL:RKU40565.1, ECO:0000313|Proteomes:UP000275385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAB683 {ECO:0000313|EMBL:RKU40565.1,
RC ECO:0000313|Proteomes:UP000275385};
RA Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. uL10 forms part of the P stalk that participates in recruiting
CC G proteins to the ribosome. {ECO:0000256|PIRNR:PIRNR039087}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000256|ARBA:ARBA00008889, ECO:0000256|PIRNR:PIRNR039087}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKU40565.1}.
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DR EMBL; QVQW01000098; RKU40565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420XY36; -.
DR STRING; 177199.A0A420XY36; -.
DR OrthoDB; 10259902at2759; -.
DR Proteomes; UP000275385; Unassembled WGS sequence.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:TreeGrafter.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:TreeGrafter.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:TreeGrafter.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:TreeGrafter.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:TreeGrafter.
DR CDD; cd05795; Ribosomal_P0_L10e; 1.
DR FunFam; 3.30.70.1730:FF:000002; 60S acidic ribosomal protein P0; 1.
DR FunFam; 3.90.105.20:FF:000001; 60S acidic ribosomal protein P0; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR050323; Ribosomal_protein_uL10.
DR InterPro; IPR001790; Ribosomal_uL10.
DR InterPro; IPR040637; Ribosomal_uL10-like_insert.
DR InterPro; IPR043164; Ribosomal_uL10-like_insert_sf.
DR InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR InterPro; IPR030670; uL10_eukaryotes.
DR PANTHER; PTHR45699; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1.
DR PANTHER; PTHR45699:SF3; LARGE RIBOSOMAL SUBUNIT PROTEIN UL10; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR039087};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|PIRNR:PIRNR039087}.
FT DOMAIN 109..178
FT /note="Large ribosomal subunit protein uL10-like insertion"
FT /evidence="ECO:0000259|Pfam:PF17777"
FT REGION 278..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..290
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 315 AA; 33621 MW; 0519D371E6D3FA2F CRC64;
MGGKSANKAG YFDKLKGLLE DYKSIFIVSV DNVSSQQMHE IRQSLRGQGV VLMGKNTMVR
RALKTFMPDS PEYERLLPFV KGNVGFVFTN GDLKDIRDKI LLNKVAAPAR AGALAPVDVW
VPAGNTGMEP GKTSFFQALG VPTKIARGTI EITSDLKLIT AGDKVGASEA SLLNLLNISP
FTYGMGVLQV YDQGNSFPPE VLDISEEQLL KSFGTAITTI AAVSLAINFP TLPSVMHSVV
NAYKKVLAIA IETEISWPEI EELKDRIANP DAYASAAPAA AAADSGAAAA AEEKKDESEK
EDSDEDDGGF GGLFD
//
