ID   RLA1_POLPE              Reviewed;         103 AA.
AC   P27464;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=60S acidic ribosomal protein P1;
DE            Short=A1;
OS   Polyorchis penicillatus (Hydromedusa).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Capitata; Polyorchidae; Polyorchis.
OX   NCBI_TaxID=6091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2031723; DOI=10.1139/o91-032;
RA   Gallin W.J.;
RT   "Sequence of an acidic ribosomal protein from the jellyfish Polyorchis
RT   penicillatus.";
RL   Biochem. Cell Biol. 69:211-215(1991).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; M64678; AAA29791.1; -; mRNA.
DR   AlphaFoldDB; P27464; -.
DR   SMR; P27464; -.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
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_L12/P1/P2.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..103
FT                   /note="60S acidic ribosomal protein P1"
FT                   /id="PRO_0000157695"
FT   REGION          66..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   103 AA;  10606 MW;  64C1FDF1230A3F80 CRC64;
     MADSSTSELA CVYSALILHD DAITAEKMNK IISAANVNVE PYWPGLFALE GKNIGDLICN
     VGSSGPAAGA PAAGAAGGAV EEKKEEKKAE SEDESDDDMG LFD