RL6_MICAN
ID RL6_MICAN Reviewed; 189 AA.
AC B0JHY9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365};
GN Synonyms=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN OrderedLocusNames=MAE_57290;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in its
CC secondary structure. It is located near the subunit interface in the
CC base of the L7/L12 stalk, and near the tRNA binding site of the
CC peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01365}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR EMBL; AP009552; BAG05551.1; -; Genomic_DNA.
DR RefSeq; WP_002796422.1; NC_010296.1.
DR AlphaFoldDB; B0JHY9; -.
DR SMR; B0JHY9; -.
DR STRING; 449447.MAE_57290; -.
DR PaxDb; B0JHY9; -.
DR EnsemblBacteria; BAG05551; BAG05551; MAE_57290.
DR GeneID; 66707887; -.
DR KEGG; mar:MAE_57290; -.
DR eggNOG; COG0097; Bacteria.
DR HOGENOM; CLU_065464_1_2_3; -.
DR OMA; KPDPYKG; -.
DR OrthoDB; 1398618at2; -.
DR BioCyc; MAER449447:MAE_RS24960-MON; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.90.930.12; -; 2.
DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR019906; Ribosomal_L6_bac-type.
DR InterPro; IPR002358; Ribosomal_L6_CS.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR PANTHER; PTHR11655:SF14; PTHR11655:SF14; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR PRINTS; PR00059; RIBOSOMALL6.
DR SUPFAM; SSF56053; SSF56053; 2.
DR TIGRFAMs; TIGR03654; L6_bact; 1.
DR PROSITE; PS00525; RIBOSOMAL_L6_1; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..189
FT /note="50S ribosomal protein L6"
FT /id="PRO_1000087050"
SQ SEQUENCE 189 AA; 20071 MW; 78C3444DBD62C2F4 CRC64;
MSRIGKRPIP IPNKVTVDID GATVTVKGPK GTLQRTLPTA VAINKDGETL LVTRQDDSRT
ARERHGLCRT LVANMVEGVA TGFQKRLDIQ GVGYRAQAQG SKLVLNVGYS KPVEMEMPDG
VSVAVENSTQ VIVSGIDKEA VGNTAAKIRE VRPPEPYKGK GIRYLGEVVR RKVGKAGGKG
AKGGKGGKK