ID RL29_HALMA Reviewed; 71 AA. AC P10971; P22526; Q5V1T1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 159. DE RecName: Full=Large ribosomal subunit protein uL29 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L29; DE AltName: Full=Hl33; DE AltName: Full=Hmal29; GN Name=rpl29; OrderedLocusNames=rrnAC1604; 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]. 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 PROTEIN SEQUENCE OF 2-70. RX PubMed=3191994; DOI=10.1016/0014-5793(88)80333-8; RA Hatakeyama T., Hatakeyama T., Kimura M.; RT "The primary structures of ribosomal proteins L16, L23 and L33 from the RT archaebacterium Halobacterium marismortui."; RL FEBS Lett. 240:21-28(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-71. RX PubMed=2143141; DOI=10.1016/0014-5793(90)80923-7; RA Arndt E.; RT "Nucleotide sequence of four genes encoding ribosomal proteins from the RT 'S10 and spectinomycin' operon equivalent region in the archaebacterium RT Halobacterium marismortui."; RL FEBS Lett. 267:193-198(1990). RN [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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: Stabilizes the tertiary rRNA structure within the 23S rRNA CC domain (domain I) to which it binds. Located at the polypeptide exit CC tunnel on the outside of the subunit. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein L23. CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 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; AAA86866.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46521.1; -; Genomic_DNA. DR EMBL; X55311; CAA39015.1; -; Genomic_DNA. DR PIR; A35064; R5HS29. DR PIR; T46794; T46794. DR RefSeq; WP_004516964.1; NZ_CP039138.1. DR PDB; 1FFK; X-ray; 2.40 A; S=2-71. DR PDB; 1JJ2; X-ray; 2.40 A; U=2-71. DR PDB; 1K73; X-ray; 3.01 A; W=2-71. DR PDB; 1K8A; X-ray; 3.00 A; W=2-71. DR PDB; 1K9M; X-ray; 3.00 A; W=2-71. DR PDB; 1KC8; X-ray; 3.01 A; W=2-71. DR PDB; 1KD1; X-ray; 3.00 A; W=2-71. DR PDB; 1KQS; X-ray; 3.10 A; U=2-71. DR PDB; 1M1K; X-ray; 3.20 A; W=2-71. DR PDB; 1M90; X-ray; 2.80 A; W=2-71. DR PDB; 1ML5; EM; 14.00 A; w=2-71. DR PDB; 1N8R; X-ray; 3.00 A; W=2-71. DR PDB; 1NJI; X-ray; 3.00 A; W=2-71. DR PDB; 1Q7Y; X-ray; 3.20 A; W=2-71. DR PDB; 1Q81; X-ray; 2.95 A; W=2-71. DR PDB; 1Q82; X-ray; 2.98 A; W=2-71. DR PDB; 1Q86; X-ray; 3.00 A; W=2-71. DR PDB; 1QVF; X-ray; 3.10 A; U=2-71. DR PDB; 1QVG; X-ray; 2.90 A; U=2-71. DR PDB; 1S72; X-ray; 2.40 A; V=1-71. DR PDB; 1VQ4; X-ray; 2.70 A; V=1-71. DR PDB; 1VQ5; X-ray; 2.60 A; V=1-71. DR PDB; 1VQ6; X-ray; 2.70 A; V=1-71. DR PDB; 1VQ7; X-ray; 2.50 A; V=1-71. DR PDB; 1VQ8; X-ray; 2.20 A; V=1-71. DR PDB; 1VQ9; X-ray; 2.40 A; V=1-71. DR PDB; 1VQK; X-ray; 2.30 A; V=1-71. DR PDB; 1VQL; X-ray; 2.30 A; V=1-71. DR PDB; 1VQM; X-ray; 2.30 A; V=1-71. DR PDB; 1VQN; X-ray; 2.40 A; V=1-71. DR PDB; 1VQO; X-ray; 2.20 A; V=1-71. DR PDB; 1VQP; X-ray; 2.25 A; V=1-71. DR PDB; 1W2B; X-ray; 3.50 A; U=2-71. DR PDB; 1YHQ; X-ray; 2.40 A; V=1-71. DR PDB; 1YI2; X-ray; 2.65 A; V=1-71. DR PDB; 1YIJ; X-ray; 2.60 A; V=1-71. DR PDB; 1YIT; X-ray; 2.80 A; V=1-71. DR PDB; 1YJ9; X-ray; 2.90 A; V=1-71. DR PDB; 1YJN; X-ray; 3.00 A; V=1-71. DR PDB; 1YJW; X-ray; 2.90 A; V=1-71. DR PDB; 2OTJ; X-ray; 2.90 A; V=1-71. DR PDB; 2OTL; X-ray; 2.70 A; V=1-71. DR PDB; 2QA4; X-ray; 3.00 A; V=1-71. DR PDB; 2QEX; X-ray; 2.90 A; V=1-71. DR PDB; 3CC2; X-ray; 2.40 A; V=1-71. DR PDB; 3CC4; X-ray; 2.70 A; V=1-71. DR PDB; 3CC7; X-ray; 2.70 A; V=1-71. DR PDB; 3CCE; X-ray; 2.75 A; V=1-71. DR PDB; 3CCJ; X-ray; 2.70 A; V=1-71. DR PDB; 3CCL; X-ray; 2.90 A; V=1-71. DR PDB; 3CCM; X-ray; 2.55 A; V=1-71. DR PDB; 3CCQ; X-ray; 2.90 A; V=1-71. DR PDB; 3CCR; X-ray; 3.00 A; V=1-71. DR PDB; 3CCS; X-ray; 2.95 A; V=1-71. DR PDB; 3CCU; X-ray; 2.80 A; V=1-71. DR PDB; 3CCV; X-ray; 2.90 A; V=1-71. DR PDB; 3CD6; X-ray; 2.75 A; V=1-71. DR PDB; 3CMA; X-ray; 2.80 A; V=1-71. DR PDB; 3CME; X-ray; 2.95 A; V=1-71. DR PDB; 3CPW; X-ray; 2.70 A; U=1-71. DR PDB; 3CXC; X-ray; 3.00 A; U=2-71. DR PDB; 3G4S; X-ray; 3.20 A; V=2-66. DR PDB; 3G6E; X-ray; 2.70 A; V=2-66. DR PDB; 3G71; X-ray; 2.85 A; V=2-66. DR PDB; 3I55; X-ray; 3.11 A; V=1-71. DR PDB; 3I56; X-ray; 2.90 A; V=1-71. DR PDB; 3OW2; X-ray; 2.70 A; U=2-66. DR PDB; 4ADX; EM; 6.60 A; V=1-71. DR PDB; 4V42; X-ray; 5.50 A; BW=2-71. DR PDB; 4V4R; X-ray; 5.90 A; 2=2-71. DR PDB; 4V4S; X-ray; 6.76 A; 2=2-71. DR PDB; 4V4T; X-ray; 6.46 A; 2=2-71. DR PDB; 4V9F; X-ray; 2.40 A; V=1-71. 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; P10971; -. DR SMR; P10971; -. DR IntAct; P10971; 3. DR STRING; 272569.rrnAC1604; -. DR PaxDb; 272569-rrnAC1604; -. DR EnsemblBacteria; AAV46521; AAV46521; rrnAC1604. DR GeneID; 64821822; -. DR KEGG; hma:rrnAC1604; -. DR PATRIC; fig|272569.17.peg.2294; -. DR eggNOG; arCOG00785; Archaea. DR HOGENOM; CLU_158491_2_2_2; -. DR EvolutionaryTrace; P10971; -. 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-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd00427; Ribosomal_L29_HIP; 1. DR Gene3D; 1.10.287.310; -; 1. DR HAMAP; MF_00374; Ribosomal_uL29; 1. DR InterPro; IPR001854; Ribosomal_uL29. DR InterPro; IPR018254; Ribosomal_uL29_CS. DR InterPro; IPR036049; Ribosomal_uL29_sf. DR NCBIfam; TIGR00012; L29; 1. DR PANTHER; PTHR10916:SF0; 50S RIBOSOMAL PROTEIN L29, CHLOROPLASTIC; 1. DR PANTHER; PTHR10916; 60S RIBOSOMAL PROTEIN L35/50S RIBOSOMAL PROTEIN L29; 1. DR Pfam; PF00831; Ribosomal_L29; 1. DR SUPFAM; SSF46561; Ribosomal protein L29 (L29p); 1. DR PROSITE; PS00579; RIBOSOMAL_L29; 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 /evidence="ECO:0000269|PubMed:3191994" FT CHAIN 2..71 FT /note="Large ribosomal subunit protein uL29" FT /id="PRO_0000130508" FT HELIX 6..11 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 14..36 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 44..64 FT /evidence="ECO:0007829|PDB:1VQ8" SQ SEQUENCE 71 AA; 7879 MW; 31779CA339CC699A CRC64; MTVLHVQEIR DMTPAEREAE LDDLKTELLN ARAVQAAGGA PENPGRIKEL RKAIARIKTI QGEEGDLQEN E //