ID   RS2_URECA               Reviewed;         278 AA.
AC   P49154;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=40S ribosomal protein S2;
GN   Name=RPS2;
OS   Urechis caupo (Innkeeper worm) (Spoonworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Echiura; Xenopneusta; Urechidae; Urechis.
OX   NCBI_TaxID=6431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8111976; DOI=10.1002/dvg.1020140609;
RA   Rosenthal E.T.;
RT   "Sequence analysis of translationally controlled maternal mRNAs from
RT   Urechis caupo.";
RL   Dev. Genet. 14:485-491(1993).
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; U30454; AAA74095.1; -; mRNA.
DR   AlphaFoldDB; P49154; -.
DR   SMR; P49154; -.
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   2: Evidence at transcript level;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..278
FT                   /note="40S ribosomal protein S2"
FT                   /id="PRO_0000131681"
FT   DOMAIN          88..151
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  30063 MW;  27EA931E8B1218F2 CRC64;
     MADAPAPAGG RGGFRGGFGG RGRGRGRGRG RGRGRGRGAK DGDKEWVPVT KLGRLVKDMK
     IKTLEEIYLF SLPIKEFEII DFFLGDALKD EVLKIMPVQK QTRAGQRTRF KAFVAIGDYN
     GHVGLGVKCS KEVATAIRGA IILAKLSVVP VRRGYWGNKI GKPHTVPCKV TGKCGSVLVR
     LIPAPRGTGI VSAPVPKKLL AMAGIDDCYT SARGQTATLG NFAKATYAAI AATYSYLTPD
     LWRETVFTKS PYQEYTDYLA KHHGRGAVTA HPTEEKPF