ID RL37_HALMA Reviewed; 57 AA. AC P32410; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 133. DE RecName: Full=Large ribosomal subunit protein eL37 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L37e; DE AltName: Full=L35e; GN Name=rpl37e; OrderedLocusNames=rrnAC0797.1; 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 [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 [2] RP PROTEIN SEQUENCE OF 2-57. RX PubMed=8504167; DOI=10.1016/0167-4781(93)90181-c; RA Bergmann U., Wittmann-Liebold B.; RT "HL35e and HLA: primary structure of two very basic and cysteine-rich RT ribosomal proteins from Haloarcula marismortui."; RL Biochim. Biophys. Acta 1173:195-200(1993). 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: Binds to the 23S rRNA. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with CC protein L4. {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 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; AY596297; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S33789; S33789. DR RefSeq; WP_004517916.1; NZ_CP039138.1. DR PDB; 1FFK; X-ray; 2.40 A; X=2-57. DR PDB; 1JJ2; X-ray; 2.40 A; Z=2-57. DR PDB; 1K73; X-ray; 3.01 A; 2=2-57. DR PDB; 1K8A; X-ray; 3.00 A; 2=2-57. DR PDB; 1K9M; X-ray; 3.00 A; 2=2-57. DR PDB; 1KC8; X-ray; 3.01 A; 2=2-57. DR PDB; 1KD1; X-ray; 3.00 A; 2=2-57. DR PDB; 1KQS; X-ray; 3.10 A; Z=2-57. DR PDB; 1M1K; X-ray; 3.20 A; 2=2-57. DR PDB; 1M90; X-ray; 2.80 A; 2=2-57. DR PDB; 1N8R; X-ray; 3.00 A; 2=2-57. DR PDB; 1NJI; X-ray; 3.00 A; 2=2-57. DR PDB; 1Q7Y; X-ray; 3.20 A; 2=2-57. DR PDB; 1Q81; X-ray; 2.95 A; 2=2-57. DR PDB; 1Q82; X-ray; 2.98 A; 2=2-57. DR PDB; 1Q86; X-ray; 3.00 A; 2=2-57. DR PDB; 1QVF; X-ray; 3.10 A; Z=2-57. DR PDB; 1QVG; X-ray; 2.90 A; Z=2-57. DR PDB; 1S72; X-ray; 2.40 A; 1=1-57. DR PDB; 1VQ4; X-ray; 2.70 A; 1=1-57. DR PDB; 1VQ5; X-ray; 2.60 A; 1=1-57. DR PDB; 1VQ6; X-ray; 2.70 A; 1=1-57. DR PDB; 1VQ7; X-ray; 2.50 A; 1=1-57. DR PDB; 1VQ8; X-ray; 2.20 A; 1=1-57. DR PDB; 1VQ9; X-ray; 2.40 A; 1=1-57. DR PDB; 1VQK; X-ray; 2.30 A; 1=1-57. DR PDB; 1VQL; X-ray; 2.30 A; 1=1-57. DR PDB; 1VQM; X-ray; 2.30 A; 1=1-57. DR PDB; 1VQN; X-ray; 2.40 A; 1=1-57. DR PDB; 1VQO; X-ray; 2.20 A; 1=1-57. DR PDB; 1VQP; X-ray; 2.25 A; 1=1-57. DR PDB; 1W2B; X-ray; 3.50 A; Z=2-57. DR PDB; 1YHQ; X-ray; 2.40 A; 1=1-57. DR PDB; 1YI2; X-ray; 2.65 A; 1=1-57. DR PDB; 1YIJ; X-ray; 2.60 A; 1=1-57. DR PDB; 1YIT; X-ray; 2.80 A; 1=1-57. DR PDB; 1YJ9; X-ray; 2.90 A; 1=1-57. DR PDB; 1YJN; X-ray; 3.00 A; 1=1-57. DR PDB; 1YJW; X-ray; 2.90 A; 1=1-57. DR PDB; 2OTJ; X-ray; 2.90 A; 1=1-57. DR PDB; 2OTL; X-ray; 2.70 A; 1=1-57. DR PDB; 2QA4; X-ray; 3.00 A; 1=1-57. DR PDB; 2QEX; X-ray; 2.90 A; 1=1-57. DR PDB; 3CC2; X-ray; 2.40 A; 1=1-57. DR PDB; 3CC4; X-ray; 2.70 A; 1=1-57. DR PDB; 3CC7; X-ray; 2.70 A; 1=1-57. DR PDB; 3CCE; X-ray; 2.75 A; 1=1-57. DR PDB; 3CCJ; X-ray; 2.70 A; 1=1-57. DR PDB; 3CCL; X-ray; 2.90 A; 1=1-57. DR PDB; 3CCM; X-ray; 2.55 A; 1=1-57. DR PDB; 3CCQ; X-ray; 2.90 A; 1=1-57. DR PDB; 3CCR; X-ray; 3.00 A; 1=1-57. DR PDB; 3CCS; X-ray; 2.95 A; 1=1-57. DR PDB; 3CCU; X-ray; 2.80 A; 1=1-57. DR PDB; 3CCV; X-ray; 2.90 A; 1=1-57. DR PDB; 3CD6; X-ray; 2.75 A; 1=1-57. DR PDB; 3CMA; X-ray; 2.80 A; 1=1-57. DR PDB; 3CME; X-ray; 2.95 A; 1=1-57. DR PDB; 3CPW; X-ray; 2.70 A; Z=1-57. DR PDB; 3CXC; X-ray; 3.00 A; Z=2-57. DR PDB; 3G4S; X-ray; 3.20 A; 1=2-57. DR PDB; 3G6E; X-ray; 2.70 A; 1=2-57. DR PDB; 3G71; X-ray; 2.85 A; 1=2-57. DR PDB; 3I55; X-ray; 3.11 A; 1=1-57. DR PDB; 3I56; X-ray; 2.90 A; 1=1-57. DR PDB; 3OW2; X-ray; 2.70 A; Z=2-57. DR PDB; 4ADX; EM; 6.60 A; 1=1-57. DR PDB; 4V9F; X-ray; 2.40 A; 1=1-57. 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; 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; 4V9F; -. DR AlphaFoldDB; P32410; -. DR SMR; P32410; -. DR IntAct; P32410; 2. DR GeneID; 64822544; -. DR EvolutionaryTrace; P32410; -. 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR Gene3D; 2.20.25.30; -; 1. DR HAMAP; MF_00547; Ribosomal_eL37; 1. DR InterPro; IPR001569; Ribosomal_eL37. DR InterPro; IPR011331; Ribosomal_eL37/eL43. DR InterPro; IPR018267; Ribosomal_eL37_CS. DR InterPro; IPR011332; Ribosomal_zn-bd. DR PANTHER; PTHR10768; 60S RIBOSOMAL PROTEIN L37; 1. DR PANTHER; PTHR10768:SF0; RIBOSOMAL PROTEIN L37; 1. DR Pfam; PF01907; Ribosomal_L37e; 1. DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1. DR PROSITE; PS01077; RIBOSOMAL_L37E; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8504167" FT CHAIN 2..57 FT /note="Large ribosomal subunit protein eL37" FT /id="PRO_0000139726" FT ZN_FING 20..38 FT /note="C4-type" FT /evidence="ECO:0000305" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 30..33 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:1VQ8" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:1VQ8" SQ SEQUENCE 57 AA; 6314 MW; A21A05AACA3112EC CRC64; MTGAGTPSQG KKNTTTHTKC RRCGEKSYHT KKKVCSSCGF GKSAKRRDYE WQSKAGE //