ID   RSSA1_VANPO             Reviewed;         252 AA.
AC   A7TEU3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=40S ribosomal protein S0-A {ECO:0000255|HAMAP-Rule:MF_03015};
GN   Name=RPS0A {ECO:0000255|HAMAP-Rule:MF_03015}; ORFNames=Kpol_1050p46;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480381; EDO19189.1; -; Genomic_DNA.
DR   RefSeq; XP_001647047.1; XM_001646997.1.
DR   AlphaFoldDB; A7TEU3; -.
DR   SMR; A7TEU3; -.
DR   STRING; 436907.A7TEU3; -.
DR   EnsemblFungi; EDO19189; EDO19189; Kpol_1050p46.
DR   GeneID; 5547520; -.
DR   KEGG; vpo:Kpol_1050p46; -.
DR   eggNOG; KOG0830; Eukaryota.
DR   HOGENOM; CLU_058171_2_0_1; -.
DR   InParanoid; A7TEU3; -.
DR   OMA; ENKMKRY; -.
DR   OrthoDB; 1129610at2759; -.
DR   PhylomeDB; A7TEU3; -.
DR   Proteomes; UP000000267; 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; Reference proteome; Ribonucleoprotein;
KW   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_0000371651"
FT   REGION          209..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
SQ   SEQUENCE   252 AA;  27932 MW;  26EB4CB67AA5A4FA CRC64;
     MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNT RPDGVNVINV GKTWEKIVLA
     ARIIAAIPNP EDVCAISSRT YGQRAVLKFS AHTGATPIAG RFTPGSFTNY ITRSFKEPRL
     IIVTDPRSDF QAIKEASYVN IPVIALTDLD SPSEYVDVAI PCNNRGKHSI GLVWYLLARE
     VLRLRGALVD RTQPWAIMPD LYFYRNPEEV EQQAAEETTS TGADAEESKE EVAEGQNEAS
     EWAEENTEAV SW