ID B2YI02_9BILA Unreviewed; 109 AA.
AC B2YI02;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|ARBA:ARBA00041116};
DE AltName: Full=60S acidic ribosomal protein P1 {ECO:0000256|ARBA:ARBA00042918};
OS Novocrania anomala.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Craniiformea;
OC Craniata; Craniida; Cranioidea; Craniidae; Novocrania.
OX NCBI_TaxID=317945 {ECO:0000313|EMBL:ACD65133.1};
RN [1] {ECO:0000313|EMBL:ACD65133.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18495619; DOI=10.1098/rspb.2008.0372;
RA Helmkampf M., Bruchhaus I., Hausdorf B.;
RT "Phylogenomic analyses of lophophorates (brachiopods, phoronids and
RT bryozoans) confirm the Lophotrochozoa concept.";
RL Proc. R. Soc. B 275:1927-1933(2008).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis. {ECO:0000256|ARBA:ARBA00003362}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000256|ARBA:ARBA00005436}.
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DR EMBL; EU558330; ACD65133.1; -; mRNA.
DR AlphaFoldDB; B2YI02; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:UniProt.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR CDD; cd05831; Ribosomal_P1; 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 PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 2: Evidence at transcript level;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000313|EMBL:ACD65133.1}.
FT REGION 65..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 109 AA; 11326 MW; 747974DD0B49F984 CRC64;
MASKDELACT YSALILADDD IAITAEKIST ILKAANVNVE PFWPGLFAKA LDGISVRDLI
SNVGSASAAP AAGGGATAGG EEKKEEAKVE EKKEESEESD DDMGFGLFD
//
