ID   RSSA1_YEAS1             Reviewed;         252 AA.
AC   B3LI22;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=40S ribosomal protein S0-A {ECO:0000255|HAMAP-Rule:MF_03015};
DE   AltName: Full=Nucleic acid-binding protein NAB1A;
GN   Name=RPS0A {ECO:0000255|HAMAP-Rule:MF_03015}; Synonyms=NAB1, NAB1A, YST1;
GN   ORFNames=SCRG_00807;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC       ribosomal subunit. Required for the processing of the 20S rRNA-
CC       precursor to mature 18S rRNA in a late step of the maturation of 40S
CC       ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (25S, 5.8S and 5S). Interacts with RPS21. {ECO:0000255|HAMAP-
CC       Rule:MF_03015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408044; EDV10043.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LI22; -.
DR   SMR; B3LI22; -.
DR   IntAct; B3LI22; 1.
DR   PRIDE; B3LI22; -.
DR   EnsemblFungi; EDV10043; EDV10043; SCRG_00807.
DR   HOGENOM; CLU_058171_2_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01425; RPS2; 1.
DR   HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR   InterPro; IPR001865; Ribosomal_S2.
DR   InterPro; IPR018130; Ribosomal_S2_CS.
DR   InterPro; IPR027498; Ribosomal_S2_euk.
DR   InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR   InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR   PANTHER; PTHR11489; PTHR11489; 1.
DR   Pfam; PF00318; Ribosomal_S2; 2.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF52313; SSF52313; 1.
DR   TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR   PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT   CHAIN           2..252
FT                   /note="40S ribosomal protein S0-A"
FT                   /id="PRO_0000371645"
FT   REGION          209..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32905, ECO:0000255|HAMAP-
FT                   Rule:MF_03015"
SQ   SEQUENCE   252 AA;  28024 MW;  D6F263456282C771 CRC64;
     MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNA RPDGVHVINV GKTWEKLVLA
     ARIIAAIPNP EDVVAISSRT FGQRAVLKFA AHTGATPIAG RFTPGSFTNY ITRSFKEPRL
     VIVTDPRSDA QAIKEASYVN IPVIALTDLD SPSEFVDVAI PCNNRGKHSI GLIWYLLARE
     VLRLRGALVD RTQPWSIMPD LYFYRDPEEV EQQVAEEATT EEAGEEEAKE EVTEEQAEAT
     EWAEENADNV EW