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Database: UniProt
Entry: H8XBG3_CANO9
LinkDB: H8XBG3_CANO9
Original site: H8XBG3_CANO9 
ID   H8XBG3_CANO9            Unreviewed;       312 AA.
AC   H8XBG3;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN   ORFNames=CORT_0H00330 {ECO:0000313|EMBL:CCG25151.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG25151.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG25151.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
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}.
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DR   EMBL; HE681726; CCG25151.1; -; Genomic_DNA.
DR   RefSeq; XP_003871276.1; XM_003871227.1.
DR   AlphaFoldDB; H8XBG3; -.
DR   GeneID; 14542407; -.
DR   KEGG; cot:CORT_0H00330; -.
DR   eggNOG; KOG0815; Eukaryota.
DR   HOGENOM; CLU_053173_1_1_1; -.
DR   OrthoDB; 168365at2759; -.
DR   Proteomes; UP000005018; Chromosome 8.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR   CDD; cd05795; Ribosomal_P0_L10e; 1.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   Gene3D; 3.90.105.20; -; 1.
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; 60S ACIDIC RIBOSOMAL PROTEIN P0; 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   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        291..306
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   312 AA;  33270 MW;  CC0854DE0BEF6D20 CRC64;
     MGGIRDKKVQ YFAKLRELLE EYKSIFIVGV DNVSSQQMHE IRKALRDDAV VLMGKNTMVR
     RAIRGFLSEL PDYEKLLPFV KGNVGFIFTN ADLKTIRDTI TSNVVAAPAK AGAVAPADVY
     IPAGNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVE KDGKVGPSEA TLLNMLNISP
     FTYGLTVVQV YDNGQVFPAS ILDITDDELI GHFVSAINTI ASISLAAGYP TLPSVGHSLI
     NNYKNVLALS IATDYTFEGS EAIKDRLANP EAYAAAAPAA AAAGGDAEPA AEAAAEEEEE
     QSDDDMGFGL FD
//
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