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RL2_SULIK
ID   RL2_SULIK               Reviewed;         238 AA.
AC   C4KHF9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=M164_1417;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC       association of the 30S and 50S subunits to form the 70S ribosome, for
CC       tRNA binding and peptide bond formation. It has been suggested to have
CC       peptidyltransferase activity; this is somewhat controversial. Makes
CC       several contacts with the 16S rRNA in the 70S ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC       subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR   EMBL; CP001402; ACR42023.1; -; Genomic_DNA.
DR   RefSeq; WP_012711421.1; NC_012726.1.
DR   AlphaFoldDB; C4KHF9; -.
DR   SMR; C4KHF9; -.
DR   EnsemblBacteria; ACR42023; ACR42023; M164_1417.
DR   GeneID; 7814239; -.
DR   GeneID; 7939936; -.
DR   GeneID; 8761456; -.
DR   KEGG; sid:M164_1417; -.
DR   HOGENOM; CLU_036235_0_1_2; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR023672; Ribosomal_L2_arc.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR014726; Ribosomal_L2_dom3.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..238
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_1000214461"
FT   REGION          200..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  25234 MW;  2F230A37214B2B7C CRC64;
     MGKNLLQQRA GKGSPTFRSP SWLRIGKVRY PNIFGHLVGK VIDIVHNPGM NAPVAIIKLE
     NGTKFLTQAI QGLVINQKIE FGKGSPIANG NVIEIGDAPE GTIVCNVEEN FGDGGKYARS
     AGSYAVVVGK SGDKVLIKLP SDKIKAVSNK ARATVGVVAG GGVVEKPLLK AGANYWKYKV
     KAKKWPIVRG VAMNVVDHPH GGGLHQSVSR PSTVSRNAPP GRKVGHIAAR RTGRKEGK
 
 
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