ID A0A0F8B892_CERFI Unreviewed; 312 AA.
AC A0A0F8B892;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN ORFNames=CFO_g472 {ECO:0000313|EMBL:KKF97175.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF97175.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF97175.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF97175.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) 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:KKF97175.1}.
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DR EMBL; LBBL01000014; KKF97175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8B892; -.
DR OrthoDB; 591228at147550; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:EnsemblFungi.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:EnsemblFungi.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
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:UP000034841};
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 279..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 33301 MW; 6ED0A7B23299DBB5 CRC64;
MGGKTANKAG YFDKLKGLLE EYKSIFIVSV DNVSSQQMHE IRASLRGKGV VLMGKNTMVR
RALRTFISDS PEYEALLPHI KGNIGFVFTN DDLKDIRDKI LDNRVAAPAR AGAVAPIDVW
VPAGNTGMEP GKTSFFQALG VPTKIARGTI EITSDLKLIE ANAKVGPSEA TLLNMLNISP
FTYGLGVVQV YDQGNTFPSS VLDISEEQLL KSLSSAISTI ASISLAVSYP TLASVTHSLV
NSYKNVLAVA ISTEYSWEGI EELKDRIANP DAYAAAAPTA AAASGGAEDK AEAKAEEEEE
ASDDDMGFGL FD
//
