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Database: UniProt
Entry: A0A176VRF1_MARPO
LinkDB: A0A176VRF1_MARPO
Original site: A0A176VRF1_MARPO 
ID   A0A176VRF1_MARPO        Unreviewed;       322 AA.
AC   A0A176VRF1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN   ORFNames=AXG93_285s1150 {ECO:0000313|EMBL:OAE23458.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE23458.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE23458.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE23458.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli
CC       protein L10. {ECO:0000256|ARBA:ARBA00002200,
CC       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:OAE23458.1}.
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DR   EMBL; LVLJ01002837; OAE23458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VRF1; -.
DR   OrthoDB; 168365at2759; -.
DR   Proteomes; UP000077202; 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:UP000077202};
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          114..183
FT                   /note="Large ribosomal subunit protein uL10-like insertion"
FT                   /evidence="ECO:0000259|Pfam:PF17777"
FT   REGION          298..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..322
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  34075 MW;  D452DEA0383233D7 CRC64;
     MGFKGTKLEK KQNYDKKLCD LLEQYTQVLV CAADNVGSTQ LQGIRKGLRP DSVVLMGKNT
     MMKRSIRLHA EKTGNDAYLN LMTLLVGNVG LIFTKGDLKE VSEEVAKYKV GAPARVGLVA
     PIDVVVPPGN TGLDPSQTSF FQVLNIPTKI NKGTVEIVAP VELIHKGEKV GSSEAALLSK
     LGIRPFSYGL VVQSVYDNGS VFSPEVLDLT EDDLCARFAA GVSNVAALSL GISYPTLAAA
     PHMFANAYKN VVAVALATEY SFPQAEKVKE YLADPSKFAA AAPAAAAAVS SGSAAPAAAK
     VEEKAAEPEE ESDDDMGFGL FD
//
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