ID A0A4V3XF56_9AGAM Unreviewed; 311 AA.
AC A0A4V3XF56;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 05-FEB-2025, entry version 21.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN ORFNames=EW146_g4474 {ECO:0000313|EMBL:THH16113.1};
OS Bondarzewia mesenterica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Bondarzewia.
OX NCBI_TaxID=1095465 {ECO:0000313|EMBL:THH16113.1, ECO:0000313|Proteomes:UP000310158};
RN [1] {ECO:0000313|EMBL:THH16113.1, ECO:0000313|Proteomes:UP000310158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108281 {ECO:0000313|EMBL:THH16113.1,
RC ECO:0000313|Proteomes:UP000310158};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Bondarzewia mesenterica.";
RL Submitted (FEB-2019) 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:THH16113.1}.
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; SGPL01000174; THH16113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3XF56; -.
DR OrthoDB; 10259902at2759; -.
DR Proteomes; UP000310158; 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; 3.90.105.20: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 Reference proteome {ECO:0000313|Proteomes:UP000310158};
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 284..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 33355 MW; 2FB8461996238D7B CRC64;
MGASRSEKEA YFVKLKELIA KYPSIFIVNV DNVGSNQMHQ IRVALRGRGI VLMGKNTMVR
RALRSIIAEY PLLERLLPHV KGNIGFVFTA SELAEIRDVI IANKVAAPAR AGAFAPKDVS
IPAGNTGMEP GKTSFFQALG IPTKIARGTI EIVSDVKVVT GGSRVGPSEA TLLNMLNISP
FTYGMSVVQI YDQGNVFTPS ILDVDAQELI DRFVSGIKTI AAISLALNYP TIVSVTHSLV
NAYKNLIAIS LATDYTFEGS EKAKEFLANP EAFAVAAAPV AEAAAAAPAA EEEKEEEKEE
SDDDMGFGLF D
//