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Database: UniProt
Entry: C5MFP2_CANTT
LinkDB: C5MFP2_CANTT
Original site: C5MFP2_CANTT 
ID   C5MFP2_CANTT            Unreviewed;       313 AA.
AC   C5MFP2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN   ORFNames=CTRG_04885 {ECO:0000313|EMBL:EER31156.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31156.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER31156.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; GG692401; EER31156.1; -; Genomic_DNA.
DR   RefSeq; XP_002550588.1; XM_002550542.1.
DR   AlphaFoldDB; C5MFP2; -.
DR   STRING; 294747.C5MFP2; -.
DR   EnsemblFungi; CTRG_04885-t43_1; CTRG_04885-t43_1-p1; CTRG_04885.
DR   GeneID; 8298888; -.
DR   KEGG; ctp:CTRG_04885; -.
DR   VEuPathDB; FungiDB:CTRG_04885; -.
DR   eggNOG; KOG0815; Eukaryota.
DR   HOGENOM; CLU_053173_1_1_1; -.
DR   OrthoDB; 168365at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000002037};
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..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..313
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  33506 MW;  67B43CE0191161E5 CRC64;
     MGGAREKKVQ YFTKLRELLE EYKSIFVVGV DNVSSQQMHE IRKALRGEAV VLMGKNTMVR
     RAIRGFLSEL PEFEKLLPFV KGNVGFIFTN GDLKTIRDTV VSNVVAAPAR AGAIAPKDVW
     IPAGNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVE QDAKVGPSEA TLLNMLNISP
     FTYGMTVVQV YDNGQVFPSS ILDITDDELI SHFVSAINTI ASISLATGYP TLPSVGHSII
     NNYKNVLALS IATDYTYEGS EAVKDRLANP EAYAAAAPAA GASAGASEEA AAEEAAAEDE
     ESEDEDMGFG LFD
//
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