ID RL3_HALMA Reviewed; 338 AA. AC P20279; Q5V1S4; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 27-MAR-2024, entry version 152. DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L3; DE AltName: Full=Hl1; DE AltName: Full=Hmal3; GN Name=rpl3; OrderedLocusNames=rrnAC1611; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7; RA Arndt E., Kroemer W., Hatakeyama T.; RT "Organization and nucleotide sequence of a gene cluster coding for eight RT ribosomal proteins in the archaebacterium Halobacterium marismortui."; RL J. Biol. Chem. 265:3034-3039(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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=10937989; DOI=10.1126/science.289.5481.905; RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.; RT "The complete atomic structure of the large ribosomal subunit at 2.4 A RT resolution."; RL Science 289:905-920(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=10937990; DOI=10.1126/science.289.5481.920; RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.; RT "The structural basis of ribosome activity in peptide bond synthesis."; RL Science 289:920-930(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=11828326; DOI=10.1038/nsb758; RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.; RT "A pre-translocational intermediate in protein synthesis observed in RT crystals of enzymatically active 50S subunits."; RL Nat. Struct. Biol. 9:225-230(2002). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=11483524; DOI=10.1093/emboj/20.15.4214; RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.; RT "The kink-turn: a new RNA secondary structure motif."; RL EMBO J. 20:4214-4221(2001). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH RP FOUR MACROLIDE ANTIBIOTICS. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1; RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.; RT "The structures of four macrolide antibiotics bound to the large ribosomal RT subunit."; RL Mol. Cell 10:117-128(2002). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=12185246; DOI=10.1073/pnas.172404099; RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.; RT "Structural insights into peptide bond formation."; RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5; RA Hansen J.L., Moore P.B., Steitz T.A.; RT "Structures of five antibiotics bound at the peptidyl transferase center of RT the large ribosomal subunit."; RL J. Mol. Biol. 330:1061-1075(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT RP E SITE SUBSTRATES. RX PubMed=14561884; DOI=10.1261/rna.5120503; RA Schmeing T.M., Moore P.B., Steitz T.A.; RT "Structures of deacylated tRNA mimics bound to the E site of the large RT ribosomal subunit."; RL RNA 9:1345-1352(2003). RN [11] 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: One of the primary rRNA binding proteins, it binds directly CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S CC subunit. {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L14 and L24e. Interacts weakly with protein L13. CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family. CC {ECO:0000305}. 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; J05222; AAA86859.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46528.1; -; Genomic_DNA. DR PIR; C35063; R5HS3L. DR RefSeq; WP_004957423.1; NZ_CP039138.1. DR PDB; 1FFK; X-ray; 2.40 A; B=2-338. DR PDB; 1JJ2; X-ray; 2.40 A; B=2-338. DR PDB; 1K73; X-ray; 3.01 A; D=2-338. DR PDB; 1K8A; X-ray; 3.00 A; D=2-338. DR PDB; 1K9M; X-ray; 3.00 A; D=2-338. DR PDB; 1KC8; X-ray; 3.01 A; D=2-338. DR PDB; 1KD1; X-ray; 3.00 A; D=2-338. DR PDB; 1KQS; X-ray; 3.10 A; B=2-338. DR PDB; 1M1K; X-ray; 3.20 A; D=2-338. DR PDB; 1M90; X-ray; 2.80 A; D=2-338. DR PDB; 1ML5; EM; 14.00 A; e=2-311, e=312-338. DR PDB; 1N8R; X-ray; 3.00 A; D=2-338. DR PDB; 1NJI; X-ray; 3.00 A; D=2-338. DR PDB; 1Q7Y; X-ray; 3.20 A; D=2-338. DR PDB; 1Q81; X-ray; 2.95 A; D=2-338. DR PDB; 1Q82; X-ray; 2.98 A; D=2-338. DR PDB; 1Q86; X-ray; 3.00 A; D=2-338. DR PDB; 1QVF; X-ray; 3.10 A; B=2-338. DR PDB; 1QVG; X-ray; 2.90 A; B=2-338. DR PDB; 1S72; X-ray; 2.40 A; B=1-338. DR PDB; 1VQ4; X-ray; 2.70 A; B=1-338. DR PDB; 1VQ5; X-ray; 2.60 A; B=1-338. DR PDB; 1VQ6; X-ray; 2.70 A; B=1-338. DR PDB; 1VQ7; X-ray; 2.50 A; B=1-338. DR PDB; 1VQ8; X-ray; 2.20 A; B=1-338. DR PDB; 1VQ9; X-ray; 2.40 A; B=1-338. DR PDB; 1VQK; X-ray; 2.30 A; B=1-338. DR PDB; 1VQL; X-ray; 2.30 A; B=1-338. DR PDB; 1VQM; X-ray; 2.30 A; B=1-338. DR PDB; 1VQN; X-ray; 2.40 A; B=1-338. DR PDB; 1VQO; X-ray; 2.20 A; B=1-338. DR PDB; 1VQP; X-ray; 2.25 A; B=1-338. DR PDB; 1W2B; X-ray; 3.50 A; B=2-338. DR PDB; 1YHQ; X-ray; 2.40 A; B=1-338. DR PDB; 1YI2; X-ray; 2.65 A; B=1-338. DR PDB; 1YIJ; X-ray; 2.60 A; B=1-338. DR PDB; 1YIT; X-ray; 2.80 A; B=1-338. DR PDB; 1YJ9; X-ray; 2.90 A; B=1-338. DR PDB; 1YJN; X-ray; 3.00 A; B=1-338. DR PDB; 1YJW; X-ray; 2.90 A; B=1-338. DR PDB; 2OTJ; X-ray; 2.90 A; B=1-338. DR PDB; 2OTL; X-ray; 2.70 A; B=2-338. DR PDB; 2QA4; X-ray; 3.00 A; B=1-338. DR PDB; 2QEX; X-ray; 2.90 A; B=1-338. DR PDB; 3CC2; X-ray; 2.40 A; B=1-338. DR PDB; 3CC4; X-ray; 2.70 A; B=1-338. DR PDB; 3CC7; X-ray; 2.70 A; B=1-338. DR PDB; 3CCE; X-ray; 2.75 A; B=1-338. DR PDB; 3CCJ; X-ray; 2.70 A; B=1-338. DR PDB; 3CCL; X-ray; 2.90 A; B=1-338. DR PDB; 3CCM; X-ray; 2.55 A; B=1-338. DR PDB; 3CCQ; X-ray; 2.90 A; B=1-338. DR PDB; 3CCR; X-ray; 3.00 A; B=1-338. DR PDB; 3CCS; X-ray; 2.95 A; B=1-338. DR PDB; 3CCU; X-ray; 2.80 A; B=1-338. DR PDB; 3CCV; X-ray; 2.90 A; B=1-338. DR PDB; 3CD6; X-ray; 2.75 A; B=1-338. DR PDB; 3CMA; X-ray; 2.80 A; B=1-338. DR PDB; 3CME; X-ray; 2.95 A; B=1-338. DR PDB; 3CPW; X-ray; 2.70 A; B=1-338. DR PDB; 3CXC; X-ray; 3.00 A; B=2-338. DR PDB; 3G4S; X-ray; 3.20 A; B=2-338. DR PDB; 3G6E; X-ray; 2.70 A; B=2-338. DR PDB; 3G71; X-ray; 2.85 A; B=2-338. DR PDB; 3I55; X-ray; 3.11 A; B=1-338. DR PDB; 3I56; X-ray; 2.90 A; B=1-338. DR PDB; 3OW2; X-ray; 2.70 A; B=2-338. DR PDB; 4ADX; EM; 6.60 A; B=1-338. DR PDB; 4V42; X-ray; 5.50 A; BE=2-338. DR PDB; 4V4R; X-ray; 5.90 A; BE=2-338. DR PDB; 4V4S; X-ray; 6.76 A; BE=2-338. DR PDB; 4V4T; X-ray; 6.46 A; E=2-338. DR PDB; 4V9F; X-ray; 2.40 A; B=1-338. DR PDBsum; 1FFK; -. DR PDBsum; 1JJ2; -. DR PDBsum; 1K73; -. DR PDBsum; 1K8A; -. DR PDBsum; 1K9M; -. DR PDBsum; 1KC8; -. DR PDBsum; 1KD1; -. DR PDBsum; 1KQS; -. DR PDBsum; 1M1K; -. DR PDBsum; 1M90; -. DR PDBsum; 1ML5; -. DR PDBsum; 1N8R; -. DR PDBsum; 1NJI; -. DR PDBsum; 1Q7Y; -. DR PDBsum; 1Q81; -. DR PDBsum; 1Q82; -. DR PDBsum; 1Q86; -. DR PDBsum; 1QVF; -. DR PDBsum; 1QVG; -. 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; 1W2B; -. 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; 3CPW; -. DR PDBsum; 3CXC; -. DR PDBsum; 3G4S; -. DR PDBsum; 3G6E; -. DR PDBsum; 3G71; -. DR PDBsum; 3I55; -. DR PDBsum; 3I56; -. DR PDBsum; 3OW2; -. DR PDBsum; 4ADX; -. DR PDBsum; 4V42; -. DR PDBsum; 4V4R; -. DR PDBsum; 4V4S; -. DR PDBsum; 4V4T; -. DR PDBsum; 4V9F; -. DR AlphaFoldDB; P20279; -. DR SMR; P20279; -. DR IntAct; P20279; 3. DR STRING; 272569.rrnAC1611; -. DR PaxDb; 272569-rrnAC1611; -. DR EnsemblBacteria; AAV46528; AAV46528; rrnAC1611. DR GeneID; 64821815; -. DR KEGG; hma:rrnAC1611; -. DR PATRIC; fig|272569.17.peg.2301; -. DR eggNOG; arCOG04070; Archaea. DR HOGENOM; CLU_033361_2_0_2; -. DR EvolutionaryTrace; P20279; -. DR Proteomes; UP000001169; Chromosome I. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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; 3.30.1430.10; -; 1. DR Gene3D; 4.10.960.10; Ribosomal protein L3, domain 3; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_01325_A; Ribosomal_uL3_A; 1. DR InterPro; IPR045077; L3_arc_euk. DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf. DR InterPro; IPR000597; Ribosomal_uL3. DR InterPro; IPR019928; Ribosomal_uL3_arc. DR InterPro; IPR019926; Ribosomal_uL3_CS. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR03626; L3_arch; 1. DR PANTHER; PTHR11363:SF5; 60S RIBOSOMAL PROTEIN L3; 1. DR PANTHER; PTHR11363; 60S RIBOSOMAL PROTEIN L3-RELATED; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. 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 CHAIN 2..338 FT /note="Large ribosomal subunit protein uL3" FT /id="PRO_0000077207" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 151..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 206..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 312..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..234 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 244..259 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 311 FT /note="R -> P (in Ref. 1; AAA86859)" FT /evidence="ECO:0000305" FT CONFLICT 312 FT /note="F -> FF (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:1VQP" FT STRAND 42..55 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:3CCJ" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 66..76 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 80..91 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 122..135 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:3CC4" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:3CCR" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 200..206 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:1VQK" FT HELIX 215..219 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:1YIJ" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:2QA4" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:1VQK" FT STRAND 262..279 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 293..300 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 309..314 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:1VQ8" SQ SEQUENCE 338 AA; 37341 MW; 996D3BE503F4DBD4 CRC64; MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT HVVLVNDEPN SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE VWTDEFHSEL DRTLDVPEDH DPDAAEEQIR DAHEAGDLGD LRLITHTVPD AVPSVPKKKP DVMETRVGGG SVSDRLDHAL DIVEDGGEHA MNDIFRAGEY ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL GPWNPSRVRS TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG //