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}.
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; 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