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RSSA_CANTR
ID   RSSA_CANTR              Reviewed;         261 AA.
AC   Q96VK7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=40S ribosomal protein S0 {ECO:0000255|HAMAP-Rule:MF_03015};
GN   Name=RPS0 {ECO:0000255|HAMAP-Rule:MF_03015};
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CECT1005;
RX   PubMed=11447603; DOI=10.1002/yea.749;
RA   Baquero C., Montero M., Sentandreu R., Valentin E.;
RT   "Molecular cloning of the RPS0 gene from Candida tropicalis.";
RL   Yeast 18:971-980(2001).
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}.
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DR   EMBL; AJ278686; CAC44623.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96VK7; -.
DR   SMR; Q96VK7; -.
DR   VEuPathDB; FungiDB:CTMYA2_049530; -.
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; 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..261
FT                   /note="40S ribosomal protein S0"
FT                   /id="PRO_0000371626"
FT   REGION          212..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="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   261 AA;  28631 MW;  0E37A686CDA548D2 CRC64;
     MSLPASFDLT PEDAKLLLAG NVHLGSKNVQ VHNKPYVYKT RPDGVNIINI GKTWEKIVLA
     ARIIAAIPNA NDVAVCSSRT FGQRAVLKFA AHTGATAIAG RFTPGNFTNY ITRSFKEPRL
     VIVTDPRTDA QAIKESSYVN IPVIALTDMD SPSEYVDVAI PCNNKGKHSI GLIWWLLARE
     VLRSRGIIPD RTTEWSVMPD LYFYRDPEEI EQNAAEEAKA EETEEAPAAE AETEWTGETD
     DVDWADSGAT PAAEDAAASN W
 
 
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