ID   RL2_CENSY               Reviewed;         243 AA.
AC   A0RZ09;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=CENSYa_1970;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK78576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RZ09; -.
DR   SMR; A0RZ09; -.
DR   STRING; 414004.CENSYa_1970; -.
DR   EnsemblBacteria; ABK78576; ABK78576; CENSYa_1970.
DR   KEGG; csy:CENSYa_1970; -.
DR   PATRIC; fig|414004.10.peg.1803; -.
DR   HOGENOM; CLU_036235_0_1_2; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000000758; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..243
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000310043"
FT   REGION          202..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   243 AA;  25893 MW;  8D56F1687000EE7C CRC64;
     MGKRPLVRRR GRGGMQFRAA TTGKIARAKY PAFELGEQRE GTVIDLVHER GRDAPLAKIR
     FEDGIVSYVP AVLGTRVGSS MNFGLKSEIR DGNVISVQNI PDGTTVCNVE KHYGDGGAIV
     KSAGGNATVF SHGEGGVVLK LPSGRFSTLN PKNRAMVGTL AGGGVSERPF MSAGGKWRRF
     RSKGRKYPIV RGVAQAAYVH PHGGGRHQHV GQSSTVSRNA PPGAKVGSIA ARKTGRAKIK
     DRR