ID A0A0A2L8B2_PENIT Unreviewed; 312 AA.
AC A0A0A2L8B2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN ORFNames=PITC_081120 {ECO:0000313|EMBL:KGO75426.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75426.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO75426.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75426.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO75426.1}.
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DR EMBL; JQGA01000470; KGO75426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L8B2; -.
DR STRING; 40296.A0A0A2L8B2; -.
DR HOGENOM; CLU_053173_1_1_1; -.
DR OMA; DMNPFKL; -.
DR OrthoDB; 168365at2759; -.
DR PhylomeDB; A0A0A2L8B2; -.
DR Proteomes; UP000030104; 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:UP000030104};
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 286..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 33125 MW; F350DDD2A01D997F CRC64;
MGGKSATKAA YFEKLRALLN EYSTIFIVGV DNVSSQQMHE IRISLRGEAV VLMGKNTMVR
RALKGFVTEN PEWERLLPFV RGNVGFIFTN GDLKSTKEKI LANRVAAPAR AGAIAPDDVW
IPAGNTGMEP GKTAFFQALG VPTKIARGTI EIVSDLKLVE AGNKVGASEA TLLNLLNISP
FTYGMTITQV YENGQCFGAD ILDITDEQLL AAFSQAIATI TAVSLGANYP TLPSVIHSII
NGYKKVLAAA ISTDYSWAEI DDLKDRIANP DAYASAAPVA AAATSGGDAP AAAAPAEEEE
ESDEDMGFGL FD
//
