ID RL30_HALMA Reviewed; 154 AA. AC P14121; Q5V1U3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 02-JUN-2021, entry version 146. DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371}; DE AltName: Full=Hl16; DE AltName: Full=Hl20; DE AltName: Full=Hmal30; GN Name=rpl30 {ECO:0000255|HAMAP-Rule:MF_01371}; OrderedLocusNames=rrnAC1591; 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 PROTEIN SEQUENCE. RX PubMed=2591382; DOI=10.1111/j.1432-1033.1989.tb15166.x; RA Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.; RT "Primary structures of five ribosomal proteins from the archaebacterium RT Halobacterium marismortui and their structural relationships to eubacterial RT and eukaryotic ribosomal proteins."; RL Eur. J. Biochem. 185:685-693(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1832208; DOI=10.1007/bf00282450; RA Scholzen T., Arndt E.; RT "Organization and nucleotide sequence of ten ribosomal protein genes from RT the region equivalent to the spectinomycin operon in the archaebacterium RT Halobacterium marismortui."; RL Mol. Gen. Genet. 228:70-80(1991). RN [3] 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 [4] RP PROTEIN SEQUENCE OF 1-30. 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 [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: This is one of 5 proteins that mediate the attachment of the CC 5S rRNA onto the large ribosomal subunit, stabilizing the orientation CC of adjacent RNA domains. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Binds 5S rRNA. CC {ECO:0000255|HAMAP-Rule:MF_01371, ECO:0000269|PubMed:12150912, CC ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family. CC {ECO:0000255|HAMAP-Rule:MF_01371}. 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; X58395; CAA41292.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46509.1; -; Genomic_DNA. DR PIR; S16543; R5HS30. DR RefSeq; WP_004957369.1; NZ_CP039138.1. DR PDB; 1FFK; X-ray; 2.40 A; T=1-154. DR PDB; 1JJ2; X-ray; 2.40 A; V=1-154. DR PDB; 1K73; X-ray; 3.01 A; X=1-154. DR PDB; 1K8A; X-ray; 3.00 A; X=1-154. DR PDB; 1K9M; X-ray; 3.00 A; X=1-154. DR PDB; 1KC8; X-ray; 3.01 A; X=1-154. DR PDB; 1KD1; X-ray; 3.00 A; X=1-154. DR PDB; 1KQS; X-ray; 3.10 A; V=1-154. DR PDB; 1M1K; X-ray; 3.20 A; X=1-154. DR PDB; 1M90; X-ray; 2.80 A; X=1-154. DR PDB; 1N8R; X-ray; 3.00 A; X=1-154. DR PDB; 1NJI; X-ray; 3.00 A; X=1-154. DR PDB; 1Q7Y; X-ray; 3.20 A; X=1-154. DR PDB; 1Q81; X-ray; 2.95 A; X=1-154. DR PDB; 1Q82; X-ray; 2.98 A; X=1-154. DR PDB; 1Q86; X-ray; 3.00 A; X=1-154. DR PDB; 1QVF; X-ray; 3.10 A; V=1-154. DR PDB; 1QVG; X-ray; 2.90 A; V=1-154. DR PDB; 1S72; X-ray; 2.40 A; W=1-154. DR PDB; 1VQ4; X-ray; 2.70 A; W=1-154. DR PDB; 1VQ5; X-ray; 2.60 A; W=1-154. DR PDB; 1VQ6; X-ray; 2.70 A; W=1-154. DR PDB; 1VQ7; X-ray; 2.50 A; W=1-154. DR PDB; 1VQ8; X-ray; 2.20 A; W=1-154. DR PDB; 1VQ9; X-ray; 2.40 A; W=1-154. DR PDB; 1VQK; X-ray; 2.30 A; W=1-154. DR PDB; 1VQL; X-ray; 2.30 A; W=1-154. DR PDB; 1VQM; X-ray; 2.30 A; W=1-154. DR PDB; 1VQN; X-ray; 2.40 A; W=1-154. DR PDB; 1VQO; X-ray; 2.20 A; W=1-154. DR PDB; 1VQP; X-ray; 2.25 A; W=1-154. DR PDB; 1W2B; X-ray; 3.50 A; V=1-154. DR PDB; 1YHQ; X-ray; 2.40 A; W=1-154. DR PDB; 1YI2; X-ray; 2.65 A; W=1-154. DR PDB; 1YIJ; X-ray; 2.60 A; W=1-154. DR PDB; 1YIT; X-ray; 2.80 A; W=1-154. DR PDB; 1YJ9; X-ray; 2.90 A; W=1-154. DR PDB; 1YJN; X-ray; 3.00 A; W=1-154. DR PDB; 1YJW; X-ray; 2.90 A; W=1-154. DR PDB; 2OTJ; X-ray; 2.90 A; W=1-154. DR PDB; 2OTL; X-ray; 2.70 A; W=1-154. DR PDB; 2QA4; X-ray; 3.00 A; W=1-154. DR PDB; 2QEX; X-ray; 2.90 A; W=1-154. DR PDB; 3CC2; X-ray; 2.40 A; W=1-154. DR PDB; 3CC4; X-ray; 2.70 A; W=1-154. DR PDB; 3CC7; X-ray; 2.70 A; W=1-154. DR PDB; 3CCE; X-ray; 2.75 A; W=1-154. DR PDB; 3CCJ; X-ray; 2.70 A; W=1-154. DR PDB; 3CCL; X-ray; 2.90 A; W=1-154. DR PDB; 3CCM; X-ray; 2.55 A; W=1-154. DR PDB; 3CCQ; X-ray; 2.90 A; W=1-154. DR PDB; 3CCR; X-ray; 3.00 A; W=1-154. DR PDB; 3CCS; X-ray; 2.95 A; W=1-154. DR PDB; 3CCU; X-ray; 2.80 A; W=1-154. DR PDB; 3CCV; X-ray; 2.90 A; W=1-154. DR PDB; 3CD6; X-ray; 2.75 A; W=1-154. DR PDB; 3CMA; X-ray; 2.80 A; W=1-154. DR PDB; 3CME; X-ray; 2.95 A; W=1-154. DR PDB; 3CPW; X-ray; 2.70 A; V=1-154. DR PDB; 3CXC; X-ray; 3.00 A; V=1-154. DR PDB; 3G4S; X-ray; 3.20 A; W=1-154. DR PDB; 3G6E; X-ray; 2.70 A; W=1-154. DR PDB; 3G71; X-ray; 2.85 A; W=1-154. DR PDB; 3I55; X-ray; 3.11 A; W=1-154. DR PDB; 3I56; X-ray; 2.90 A; W=1-154. DR PDB; 3OW2; X-ray; 2.70 A; V=1-154. DR PDB; 4ADX; EM; 6.60 A; W=1-154. DR PDB; 4V9F; X-ray; 2.40 A; W=1-154. 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 SMR; P14121; -. DR IntAct; P14121; 1. DR STRING; 272569.rrnAC1591; -. DR EnsemblBacteria; AAV46509; AAV46509; rrnAC1591. DR GeneID; 40152556; -. DR KEGG; hma:rrnAC1591; -. DR PATRIC; fig|272569.17.peg.2280; -. DR eggNOG; arCOG04086; Archaea. DR HOGENOM; CLU_055156_6_0_2; -. DR OMA; KDYITWG; -. DR EvolutionaryTrace; P14121; -. DR Proteomes; UP000001169; Chromosome I. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. 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; cd01657; Ribosomal_L7_archeal_euk; 1. DR Gene3D; 1.10.15.30; -; 1. DR Gene3D; 3.30.1390.20; -; 1. DR HAMAP; MF_01371_A; Ribosomal_L30_A; 1. DR InterPro; IPR036919; L30_ferredoxin-like_sf. DR InterPro; IPR005997; Ribosomal_L30_arc. DR InterPro; IPR023106; Ribosomal_L30_central_dom_arc. DR InterPro; IPR018038; Ribosomal_L30_CS. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR InterPro; IPR035808; Ribosomal_L7_euk_arc. DR Pfam; PF00327; Ribosomal_L30; 1. DR SUPFAM; SSF55129; SSF55129; 1. DR TIGRFAMs; TIGR01309; uL30_arch; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1..154 FT /note="50S ribosomal protein L30" FT /id="PRO_0000104622" FT REGION 114..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 122..146 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 83 FT /note="W -> L (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="Missing (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 39..47 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 59..69 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 81..87 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 93..101 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:1VQO" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 143..152 FT /evidence="ECO:0007829|PDB:1VQ8" SQ SEQUENCE 154 AA; 17042 MW; ED673F036E974C14 CRC64; MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND FVAFGEPSQE TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL LSEETTLREQ GLSPTLRLHP PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL EAMR //