ID   RS2_LEIAM               Reviewed;         265 AA.
AC   O43992;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=40S ribosomal protein S2;
OS   Leishmania amazonensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/BR/73/LV78;
RA   Stewart J.C., Heard P.L., Chaudhuri G.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. Plays a role in the assembly and function of the 40S ribosomal
CC       subunit. Mutations in this protein affects the control of translational
CC       fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC       ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; AF038379; AAB94922.1; -; Genomic_DNA.
DR   AlphaFoldDB; O43992; -.
DR   SMR; O43992; -.
DR   VEuPathDB; TriTrypDB:LAMA_000290100; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..265
FT                   /note="40S ribosomal protein S2"
FT                   /id="PRO_0000131680"
FT   DOMAIN          88..151
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  28703 MW;  8D704D3360D45B22 CRC64;
     MADTQPAQEA PAADAPRAER NFGRGRGGRG GRGRGRGGPG EEKEWVPCTK LGRLVKAQKV
     TSLEEIFLFS MPIKEHQIVD TLIAEGKLHD EMMKIYPVQK ATSAGQRTRF KAFNVVGDCD
     GHIGIGARVG KEVSLAIRAS MIAAKLNIVP VRRGYWGNKI GEPHTIPMKV TGKCGSVAVR
     LVPAPRGTGI VAAPVPKKIL EFAGVEDVYT SSRGKTRTHG NLIMATFYAL RKTYGFLTPD
     LWADTEPSRD PTDEHGELLA EMTTA