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Database: UniProt
Entry: A0A0D2LBT3_9CHLO
LinkDB: A0A0D2LBT3_9CHLO
Original site: A0A0D2LBT3_9CHLO 
ID   A0A0D2LBT3_9CHLO        Unreviewed;       107 AA.
AC   A0A0D2LBT3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   SubName: Full=60S acidic ribosomal protein P2-4 {ECO:0000313|EMBL:KIZ04174.1};
GN   ORFNames=MNEG_3778 {ECO:0000313|EMBL:KIZ04174.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ04174.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIZ04174.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ04174.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis. {ECO:0000256|ARBA:ARBA00003362}.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00011266}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000256|ARBA:ARBA00005436}.
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DR   EMBL; KK100711; KIZ04174.1; -; Genomic_DNA.
DR   RefSeq; XP_013903193.1; XM_014047739.1.
DR   AlphaFoldDB; A0A0D2LBT3; -.
DR   STRING; 145388.A0A0D2LBT3; -.
DR   GeneID; 25736656; -.
DR   KEGG; mng:MNEG_3778; -.
DR   OrthoDB; 5485067at2759; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR   CDD; cd05833; Ribosomal_P2; 1.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_P1/P2.
DR   InterPro; IPR044076; Ribosomal_P2.
DR   PANTHER; PTHR21141; 60S ACIDIC RIBOSOMAL PROTEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR21141:SF5; 60S ACIDIC RIBOSOMAL PROTEIN P2; 1.
DR   Pfam; PF00428; Ribosomal_60s; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:KIZ04174.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..107
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002263693"
FT   REGION          65..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   107 AA;  10903 MW;  D8B98DB865589BFF CRC64;
     MRVVSAVLLA VLGGKANPTE DDVKKILGSV GVEADADSVQ RLLKELEGKD IAELIAAGRE
     KLQSVPSGGA AAAAPAAGGA APAAKKEEAK KEEPSEEDED MGFSLFD
//
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