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Database: UniProt
Entry: K9FP11_PEND2
LinkDB: K9FP11_PEND2
Original site: K9FP11_PEND2 
ID   K9FP11_PEND2            Unreviewed;       312 AA.
AC   K9FP11;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN   ORFNames=PDIG_50770 {ECO:0000313|EMBL:EKV11360.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV11360.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(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}.
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:EKV11360.1}.
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DR   EMBL; AKCT01000206; EKV11360.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9FP11; -.
DR   STRING; 1170229.K9FP11; -.
DR   eggNOG; KOG0815; Eukaryota.
DR   HOGENOM; CLU_053173_1_1_1; -.
DR   InParanoid; K9FP11; -.
DR   OMA; DMNPFKL; -.
DR   OrthoDB; 168365at2759; -.
DR   Proteomes; UP000009882; 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:UP000009882};
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;  33191 MW;  7C9A3326CAFB9124 CRC64;
     MGGKSATKTA YFEKLRTLLN EYSTIFIVGV DNVSSQQMHE IRMALRGEAV VLMGKNTMVR
     RALKGFVTEN PEWERLLPHV RGNVGFIFTK GDLKATKEKI LANRVAAPAR AGAVAPDDVW
     VPAGNTGMEP GKTAFFQALG VPTKIARGTI EIVSDLKLVE AGNKVGASEA TLLNLLNISP
     FTYGMTITQV YENGQCFSAD VLDITDEQLL AAFSQAIATI TAVSLAANYP TLPSVIHSLI
     NGYKKVLAAA ISTDYSWAEI EDLKDRIANP DAYASAAPVA AAATSGGDAP AAAAPAEEEE
     ESDEDMGFGL FD
//
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