ID   RLA3_CANAX              Reviewed;         108 AA.
AC   Q9HFQ6;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=60S acidic ribosomal protein P1-B;
DE            Short=CaRP1B;
GN   Name=RPP1B;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476 {ECO:0000312|EMBL:AAG33241.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RA   Abramczyk D., Tchorzewski M., Grankowski N.;
RT   "Cloning, expression and purification of the acidic ribosomal protein from
RT   Candida albicans.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=15182941; DOI=10.1016/j.bbagen.2004.04.005;
RA   Abramczyk D., Tchorzewski M., Krokowski D., Boguszewska A., Grankowski N.;
RT   "Overexpression, purification and characterization of the acidic ribosomal
RT   P-proteins from Candida albicans.";
RL   Biochim. Biophys. Acta 1672:214-223(2004).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis. {ECO:0000250|UniProtKB:P17478}.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF317660; AAG33241.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HFQ6; -.
DR   VEuPathDB; FungiDB:C7_03920C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05722; -.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:EnsemblFungi.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:CAFA.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:CAFA.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..108
FT                   /note="60S acidic ribosomal protein P1-B"
FT                   /id="PRO_0000157704"
FT   REGION          72..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..108
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   108 AA;  10746 MW;  C1A21B9F6C2635DE CRC64;
     MSTEASVSYA ALILADAEQE ITSEKLLAIT KAAGANVDQV WADVFAKAVE GKNLKELLFS
     FAAAAPASGA AAGSASGAAA GGEAAAEEAA EEEAAEESDD DMGFGLFD