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Database: UniProt
Entry: A0A4V3XF56_9AGAM
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Original site: A0A4V3XF56_9AGAM 
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}.
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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
//
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