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Database: UniProt
Entry: A0A2K3QNU8_9HYPO
LinkDB: A0A2K3QNU8_9HYPO
Original site: A0A2K3QNU8_9HYPO 
ID   A0A2K3QNU8_9HYPO        Unreviewed;       108 AA.
AC   A0A2K3QNU8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=60S acidic ribosomal protein P2 {ECO:0000313|EMBL:PNY29201.1};
GN   ORFNames=TCAP_00882 {ECO:0000313|EMBL:PNY29201.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY29201.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY29201.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY29201.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PNY29201.1}.
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DR   EMBL; NRSZ01000143; PNY29201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3QNU8; -.
DR   STRING; 45235.A0A2K3QNU8; -.
DR   OrthoDB; 5485067at2759; -.
DR   Proteomes; UP000236621; 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:UP000236621};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:PNY29201.1}.
FT   REGION          62..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..108
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   108 AA;  10800 MW;  99AB723E1351F895 CRC64;
     MKHLAAYLLL GLGGNASPSS KDVKAVLSSV GIEADDERLN KLISELKGKD INELIAAGSE
     KLASVPSGGS APAAGAAAAA GGAAAEAPAE EEEEKEESDE DMGFGLFD
//
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