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Database: UniProt
Entry: G4UAY1_NEUT9
LinkDB: G4UAY1_NEUT9
Original site: G4UAY1_NEUT9 
ID   G4UAY1_NEUT9            Unreviewed;       110 AA.
AC   G4UAY1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Large ribosomal subunit protein P2 {ECO:0000256|ARBA:ARBA00035301};
DE   AltName: Full=60S acidic ribosomal protein P2 {ECO:0000256|ARBA:ARBA00035443};
GN   ORFNames=NEUTE2DRAFT_142664 {ECO:0000313|EMBL:EGZ77029.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77029.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ77029.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
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; GL890999; EGZ77029.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4UAY1; -.
DR   STRING; 510952.G4UAY1; -.
DR   eggNOG; KOG3449; Eukaryota.
DR   HOGENOM; CLU_114656_0_2_1; -.
DR   Proteomes; UP000008513; 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; IPR001859; Ribosomal_P1/P2_euk.
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.
DR   PRINTS; PR00456; RIBOSOMALP2.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:EGZ77029.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..110
FT                   /note="Large ribosomal subunit protein P2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003469455"
FT   REGION          62..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   110 AA;  11102 MW;  F6D864D236565581 CRC64;
     MKHLAAYLLL TLGGNTAPSA ADVKAVLESV GIEADSERLD KLISELEGKD LNELIAEGSS
     KLASVPSGGA AAPAAGGAAA AAGGAAEEKK EEKVEEKEES DEDMGFGLFD
//
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