RL2_PYRFU
ID RL2_PYRFU Reviewed; 239 AA.
AC Q8U001;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE AltName: Full=Large ribosomal subunit protein uL2;
GN Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=PF1822;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2] {ECO:0007744|PDB:4V6U}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS) IN THE 70S RIBOSOME, AND
RP SUBUNIT.
RX PubMed=23222135; DOI=10.1093/nar/gks1259;
RA Armache J.P., Anger A.M., Marquez V., Franckenberg S., Frohlich T.,
RA Villa E., Berninghausen O., Thomm M., Arnold G.J., Beckmann R.,
RA Wilson D.N.;
RT "Promiscuous behaviour of archaeal ribosomal proteins: implications for
RT eukaryotic ribosome evolution.";
RL Nucleic Acids Res. 41:1284-1293(2013).
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 (PubMed:23222135). Forms a
CC bridge to the 30S subunit in the 70S ribosome. {ECO:0000255|HAMAP-
CC Rule:MF_01320, ECO:0000269|PubMed:23222135}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AE009950; AAL81946.1; -; Genomic_DNA.
DR RefSeq; WP_011012963.1; NZ_CP023154.1.
DR PDB; 4V4N; EM; 9.00 A; B=1-239.
DR PDB; 4V6U; EM; 6.60 A; BB=1-239.
DR PDBsum; 4V4N; -.
DR PDBsum; 4V6U; -.
DR AlphaFoldDB; Q8U001; -.
DR SMR; Q8U001; -.
DR STRING; 186497.PF1822; -.
DR PRIDE; Q8U001; -.
DR EnsemblBacteria; AAL81946; AAL81946; PF1822.
DR GeneID; 41713641; -.
DR KEGG; pfu:PF1822; -.
DR PATRIC; fig|186497.12.peg.1893; -.
DR eggNOG; arCOG04067; Archaea.
DR HOGENOM; CLU_036235_0_1_2; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 74812at2157; -.
DR PhylomeDB; Q8U001; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..239
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129723"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 26037 MW; D260820A754EAFB6 CRC64;
MGKSLIQQRR GKGSPTFKSP SHRFRGAVKY IPLNYTQEKT LRGVVEEIMH DPGRTAPVAR
VKFENGIEKL IIAPEGLLVG QEIYIGPDAP IAVGNTLPLA KIPEGTYVYN IEGIPGDGGK
YVRAGGTYAL VVSREPDKVI VQLPSGELKA FNPMCRATIG VVAGGGRLEK PLVKAGKAYY
KYKARNKFWP TPRGVKMNAV NHPFGGKEHH PGKPTTTSRR APPGRKVGHI AARRTGRRK
