ID RL11_HALMA Reviewed; 162 AA. AC P14122; Q5V2B0; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 159. DE RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000255|HAMAP-Rule:MF_00736}; DE AltName: Full=50S ribosomal protein L11 {ECO:0000305}; DE AltName: Full=HmaL11 {ECO:0000303|PubMed:2320419}; DE AltName: Full=L10 {ECO:0000303|PubMed:3196689}; GN Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=rrnAC1414; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Halobacteria; Halobacteriales; Haloarculaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2320419; DOI=10.1093/nar/18.5.1285; RA Arndt E., Weigel C.; RT "Nucleotide sequence of the genes encoding the L11, L1, L10 and L12 RT equivalent ribosomal proteins from the archaebacterium Halobacterium RT marismortui."; RL Nucleic Acids Res. 18:1285-1285(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=15520287; DOI=10.1101/gr.2700304; RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., RA Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the RT Dead Sea."; RL Genome Res. 14:2221-2234(2004). RN [3] RP PROTEIN SEQUENCE OF 2-28, AND SUBUNIT. RX PubMed=3196689; DOI=10.1021/bi00418a032; RA Walsh M.J., McDougall J., Wittmann-Liebold B.; RT "Extended N-terminal sequencing of proteins of archaebacterial ribosomes RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene RT difluoride) membrane."; RL Biochemistry 27:6867-6876(1988). RN [4] RP 3D-STRUCTURE MODELING. RX PubMed=10476961; DOI=10.1038/23641; RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.; RT "Placement of protein and RNA structures into a 5 A-resolution map of the RT 50S ribosomal subunit."; RL Nature 400:841-847(1999). RN [5] {ECO:0007744|PDB:2QA4} RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), RRNA-BINDING, AND INTERACTION WITH RP L10. RX PubMed=17599351; DOI=10.1016/j.jmb.2007.05.091; RA Kavran J.M., Steitz T.A.; RT "Structure of the base of the L7/L12 stalk of the Haloarcula marismortui RT large ribosomal subunit: analysis of L11 movements."; RL J. Mol. Biol. 371:1047-1059(2007). RN [6] {ECO:0007744|PDB:4V9F} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. RX PubMed=23695244; DOI=10.1107/s0907444913004745; RA Gabdulkhakov A., Nikonov S., Garber M.; RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model."; RL Acta Crystallogr. D 69:997-1004(2013). CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a CC large ribonucleoprotein complex responsible for the synthesis of CC proteins in the cell. {ECO:0000305}. CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP- CC Rule:MF_00736}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:3196689). Forms part CC of the ribosomal stalk which helps the ribosome interact with GTP-bound CC translation factors. Forms a heptameric uL10-P1 complex, where uL10 CC (formerly P0) forms an elongated spine to which P1 dimers (formerly CC L12) bind in a sequential fashion (Probable). CC {ECO:0000269|PubMed:3196689, ECO:0000305|PubMed:23695244}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family. CC {ECO:0000255|HAMAP-Rule:MF_00736}. 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; X51430; CAA35793.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46342.1; -; Genomic_DNA. DR PIR; S08420; R5HS11. DR RefSeq; WP_011223608.1; NC_006396.1. DR PDB; 1C04; X-ray; 5.00 A; C=79-88. DR PDB; 1S72; X-ray; 2.40 A; I=1-162. DR PDB; 1VQ4; X-ray; 2.70 A; I=1-162. DR PDB; 1VQ5; X-ray; 2.60 A; I=1-162. DR PDB; 1VQ6; X-ray; 2.70 A; I=1-162. DR PDB; 1VQ7; X-ray; 2.50 A; I=1-162. DR PDB; 1VQ8; X-ray; 2.20 A; I=1-162. DR PDB; 1VQ9; X-ray; 2.40 A; I=1-162. DR PDB; 1VQK; X-ray; 2.30 A; I=1-162. DR PDB; 1VQL; X-ray; 2.30 A; I=1-162. DR PDB; 1VQM; X-ray; 2.30 A; I=1-162. DR PDB; 1VQN; X-ray; 2.40 A; I=1-162. DR PDB; 1VQO; X-ray; 2.20 A; I=1-162. DR PDB; 1VQP; X-ray; 2.25 A; I=1-162. DR PDB; 1YHQ; X-ray; 2.40 A; I=1-162. DR PDB; 1YI2; X-ray; 2.65 A; I=1-162. DR PDB; 1YIJ; X-ray; 2.60 A; I=1-162. DR PDB; 1YIT; X-ray; 2.80 A; I=1-162. DR PDB; 1YJ9; X-ray; 2.90 A; I=1-162. DR PDB; 1YJN; X-ray; 3.00 A; I=1-162. DR PDB; 1YJW; X-ray; 2.90 A; I=1-162. DR PDB; 2OTJ; X-ray; 2.90 A; I=2-162. DR PDB; 2OTL; X-ray; 2.70 A; I=1-162. DR PDB; 2QA4; X-ray; 3.00 A; I=1-162. DR PDB; 2QEX; X-ray; 2.90 A; I=1-162. DR PDB; 3CC2; X-ray; 2.40 A; I=1-162. DR PDB; 3CC4; X-ray; 2.70 A; I=1-162. DR PDB; 3CC7; X-ray; 2.70 A; I=1-162. DR PDB; 3CCE; X-ray; 2.75 A; I=1-162. DR PDB; 3CCJ; X-ray; 2.70 A; I=1-162. DR PDB; 3CCL; X-ray; 2.90 A; I=1-162. DR PDB; 3CCM; X-ray; 2.55 A; I=1-162. DR PDB; 3CCQ; X-ray; 2.90 A; I=1-162. DR PDB; 3CCR; X-ray; 3.00 A; I=1-162. DR PDB; 3CCS; X-ray; 2.95 A; I=1-162. DR PDB; 3CCU; X-ray; 2.80 A; I=1-162. DR PDB; 3CCV; X-ray; 2.90 A; I=1-162. DR PDB; 3CD6; X-ray; 2.75 A; I=1-162. DR PDB; 3CMA; X-ray; 2.80 A; I=1-162. DR PDB; 3CME; X-ray; 2.95 A; I=1-162. DR PDB; 3G4S; X-ray; 3.20 A; I=67-136. DR PDB; 3G6E; X-ray; 2.70 A; I=67-136. DR PDB; 3G71; X-ray; 2.85 A; I=67-136. DR PDB; 3I55; X-ray; 3.11 A; I=1-162. DR PDB; 3I56; X-ray; 2.90 A; I=1-162. DR PDB; 4V9F; X-ray; 2.40 A; I=1-162. DR AlphaFoldDB; P14122; -. DR SMR; P14122; -. DR IntAct; P14122; 1. DR STRING; 272569.rrnAC1414; -. DR PaxDb; 272569-rrnAC1414; -. DR EnsemblBacteria; AAV46342; AAV46342; rrnAC1414. DR GeneID; 40152382; -. DR KEGG; hma:rrnAC1414; -. DR PATRIC; fig|272569.17.peg.2109; -. DR eggNOG; arCOG04372; Archaea. DR HOGENOM; CLU_074237_4_0_2; -. DR EvolutionaryTrace; P14122; -. DR Proteomes; UP000001169; Chromosome I. DR GO; GO:0015934; C:large ribosomal subunit; IEA:TreeGrafter. DR GO; GO:0070180; F:large ribosomal subunit 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 CDD; cd00349; Ribosomal_L11; 1. DR FunFam; 1.10.10.250:FF:000006; 50S ribosomal protein L11; 1. DR Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1. DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1. DR HAMAP; MF_00736; Ribosomal_uL11; 1. DR InterPro; IPR000911; Ribosomal_uL11. DR InterPro; IPR020783; Ribosomal_uL11_C. DR InterPro; IPR036769; Ribosomal_uL11_C_sf. DR InterPro; IPR020785; Ribosomal_uL11_CS. DR InterPro; IPR020784; Ribosomal_uL11_N. DR InterPro; IPR036796; Ribosomal_uL11_N_sf. DR NCBIfam; NF002232; PRK01143.1; 1. DR PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1. DR PANTHER; PTHR11661:SF1; LARGE RIBOSOMAL SUBUNIT PROTEIN UL11M; 1. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR SMART; SM00649; RL11; 1. DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1. DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; 1. DR PDBsum; 1C04; -. DR PDBsum; 1S72; -. DR PDBsum; 1VQ4; -. DR PDBsum; 1VQ5; -. DR PDBsum; 1VQ6; -. DR PDBsum; 1VQ7; -. DR PDBsum; 1VQ8; -. DR PDBsum; 1VQ9; -. DR PDBsum; 1VQK; -. DR PDBsum; 1VQL; -. DR PDBsum; 1VQM; -. DR PDBsum; 1VQN; -. DR PDBsum; 1VQO; -. DR PDBsum; 1VQP; -. DR PDBsum; 1YHQ; -. DR PDBsum; 1YI2; -. DR PDBsum; 1YIJ; -. DR PDBsum; 1YIT; -. DR PDBsum; 1YJ9; -. DR PDBsum; 1YJN; -. DR PDBsum; 1YJW; -. DR PDBsum; 2OTJ; -. DR PDBsum; 2OTL; -. DR PDBsum; 2QA4; -. DR PDBsum; 2QEX; -. DR PDBsum; 3CC2; -. DR PDBsum; 3CC4; -. DR PDBsum; 3CC7; -. DR PDBsum; 3CCE; -. DR PDBsum; 3CCJ; -. DR PDBsum; 3CCL; -. DR PDBsum; 3CCM; -. DR PDBsum; 3CCQ; -. DR PDBsum; 3CCR; -. DR PDBsum; 3CCS; -. DR PDBsum; 3CCU; -. DR PDBsum; 3CCV; -. DR PDBsum; 3CD6; -. DR PDBsum; 3CMA; -. DR PDBsum; 3CME; -. DR PDBsum; 3G4S; -. DR PDBsum; 3G6E; -. DR PDBsum; 3G71; -. DR PDBsum; 3I55; -. DR PDBsum; 3I56; -. DR PDBsum; 4V9F; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3196689" FT CHAIN 2..162 FT /note="Large ribosomal subunit protein uL11" FT /id="PRO_0000104431" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:4V9F" FT TURN 18..23 FT /evidence="ECO:0007829|PDB:4V9F" FT TURN 33..36 FT /evidence="ECO:0007829|PDB:4V9F" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:4V9F" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:4V9F" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:4V9F" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:4V9F" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:4V9F" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 108..111 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 117..127 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 128..132 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 143..148 FT /evidence="ECO:0007829|PDB:4V9F" FT TURN 149..152 FT /evidence="ECO:0007829|PDB:4V9F" FT HELIX 153..156 FT /evidence="ECO:0007829|PDB:4V9F" SQ SEQUENCE 162 AA; 17089 MW; E64E6802B49208B8 CRC64; MAGTIEVLVP GGEANPGPPL GPELGPTPVD VQAVVQEIND QTAAFDGTEV PVTVKYDDDG SFEIEVGVPP TAELIKDEAG FETGSGEPQE DFVADLSVDQ VKQIAEQKHP DLLSYDLTNA AKEVVGTCTS LGVTIEGENP REFKERIDAG EYDDVFAAEA QA //