ID M0L4F0_9EURY Unreviewed; 178 AA. AC M0L4F0; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=50S ribosomal protein L6 {ECO:0000256|HAMAP-Rule:MF_01365}; GN Name=rpl6 {ECO:0000256|HAMAP-Rule:MF_01365}; GN Synonyms=rpl6p {ECO:0000313|EMBL:EMA26870.1}; GN ORFNames=C435_00145 {ECO:0000313|EMBL:EMA26870.1}; OS Haloarcula californiae ATCC 33799. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Haloarculaceae; OC Haloarcula. OX NCBI_TaxID=662475 {ECO:0000313|EMBL:EMA26870.1, ECO:0000313|Proteomes:UP000011687}; RN [1] {ECO:0000313|EMBL:EMA26870.1, ECO:0000313|Proteomes:UP000011687} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33799 {ECO:0000313|EMBL:EMA26870.1, RC ECO:0000313|Proteomes:UP000011687}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in CC its secondary structure. It is located near the subunit interface CC in the base of the L7/L12 stalk, and near the tRNA binding site of CC the peptidyltransferase center. {ECO:0000256|HAMAP-Rule:MF_01365}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP- CC Rule:MF_01365}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family. CC {ECO:0000256|HAMAP-Rule:MF_01365}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMA26870.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AOLS01000002; EMA26870.1; -; Genomic_DNA. DR RefSeq; WP_007187645.1; NZ_AOLS01000002.1. DR RefSeq; WP_007187645.1; NZ_AOLS01000002.1. DR RefSeq; WP_007187645.1; NZ_AOLS01000002.1. DR EnsemblBacteria; EMA26870; EMA26870; C435_00145. DR OrthoDB; POG093Z0CBF; -. DR Proteomes; UP000011687; Unassembled WGS sequence. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.930.12; -; 2. DR HAMAP; MF_01365_A; Ribosomal_L6_A; 1. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR020040; Ribosomal_L6_a/b-dom. DR InterPro; IPR002359; Ribosomal_L6_CS2. DR InterPro; IPR019907; Ribosomal_L6P_arc. DR PANTHER; PTHR11655; PTHR11655; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR SUPFAM; SSF56053; SSF56053; 2. DR TIGRFAMs; TIGR03653; uL6_arch; 1. DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011687}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01365}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01365, KW ECO:0000313|EMBL:EMA26870.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01365}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01365}. FT DOMAIN 8 80 Ribosomal_L6. {ECO:0000259|Pfam:PF00347}. FT DOMAIN 92 166 Ribosomal_L6. {ECO:0000259|Pfam:PF00347}. SQ SEQUENCE 178 AA; 19914 MW; 380874F38AAA7E5E CRC64; MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPAID VSVDGDTVVI ESDEDNAKTM STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG DEVVIENFLG EKAPRRTTIH GDTDVEIDGE ELTISGPDIE AVGQTAADIE QLTRINDKDV RVFQDGVYIT RKPNRGDA //