RL21_HALMA
ID RL21_HALMA Reviewed; 96 AA.
AC P12734; Q5V585;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=50S ribosomal protein L21e;
DE AltName: Full=Hl31;
GN Name=rpl21e; OrderedLocusNames=rrnAC0260;
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 2-96.
RX PubMed=3350019; DOI=10.1111/j.1432-1033.1988.tb13945.x;
RA Hatakeyama T., Kimura M.;
RT "Complete amino acid sequences of the ribosomal proteins L25, L29 and L31
RT from the archaebacterium Halobacterium marismortui.";
RL Eur. J. Biochem. 172:703-711(1988).
RN [3]
RP CROSS-LINKING TO L18.
RX PubMed=8345527; DOI=10.1006/jmbi.1993.1419;
RA Bergmann U., Wittmann-Liebold B.;
RT "Localization of proteins HL29 and HL31 from Haloarcula marismortui within
RT the 50 S ribosomal subunit by chemical crosslinking.";
RL J. Mol. Biol. 232:693-700(1993).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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. Interacts with protein L18
CC and binds the 5S rRNA. Has been cross-linked to L18.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC {ECO:0000305}.
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DR EMBL; AY596297; AAV45317.1; -; Genomic_DNA.
DR PIR; S00370; R5HS31.
DR RefSeq; WP_004962804.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; N=2-96.
DR PDB; 1JJ2; X-ray; 2.40 A; P=2-96.
DR PDB; 1K73; X-ray; 3.01 A; R=2-96.
DR PDB; 1K8A; X-ray; 3.00 A; R=2-96.
DR PDB; 1K9M; X-ray; 3.00 A; R=2-96.
DR PDB; 1KC8; X-ray; 3.01 A; R=2-96.
DR PDB; 1KD1; X-ray; 3.00 A; R=2-96.
DR PDB; 1KQS; X-ray; 3.10 A; P=2-96.
DR PDB; 1M1K; X-ray; 3.20 A; R=2-96.
DR PDB; 1M90; X-ray; 2.80 A; R=2-96.
DR PDB; 1N8R; X-ray; 3.00 A; R=2-96.
DR PDB; 1NJI; X-ray; 3.00 A; R=2-96.
DR PDB; 1Q7Y; X-ray; 3.20 A; R=2-96.
DR PDB; 1Q81; X-ray; 2.95 A; R=2-96.
DR PDB; 1Q82; X-ray; 2.98 A; R=2-96.
DR PDB; 1Q86; X-ray; 3.00 A; R=2-96.
DR PDB; 1QVF; X-ray; 3.10 A; P=2-96.
DR PDB; 1QVG; X-ray; 2.90 A; P=2-96.
DR PDB; 1S72; X-ray; 2.40 A; Q=1-96.
DR PDB; 1VQ4; X-ray; 2.70 A; Q=1-96.
DR PDB; 1VQ5; X-ray; 2.60 A; Q=1-96.
DR PDB; 1VQ6; X-ray; 2.70 A; Q=1-96.
DR PDB; 1VQ7; X-ray; 2.50 A; Q=1-96.
DR PDB; 1VQ8; X-ray; 2.20 A; Q=1-96.
DR PDB; 1VQ9; X-ray; 2.40 A; Q=1-96.
DR PDB; 1VQK; X-ray; 2.30 A; Q=1-96.
DR PDB; 1VQL; X-ray; 2.30 A; Q=1-96.
DR PDB; 1VQM; X-ray; 2.30 A; Q=1-96.
DR PDB; 1VQN; X-ray; 2.40 A; Q=1-96.
DR PDB; 1VQO; X-ray; 2.20 A; Q=1-96.
DR PDB; 1VQP; X-ray; 2.25 A; Q=1-96.
DR PDB; 1W2B; X-ray; 3.50 A; P=2-96.
DR PDB; 1YHQ; X-ray; 2.40 A; Q=1-96.
DR PDB; 1YI2; X-ray; 2.65 A; Q=1-96.
DR PDB; 1YIJ; X-ray; 2.60 A; Q=1-96.
DR PDB; 1YIT; X-ray; 2.80 A; Q=1-96.
DR PDB; 1YJ9; X-ray; 2.90 A; Q=1-96.
DR PDB; 1YJN; X-ray; 3.00 A; Q=1-96.
DR PDB; 1YJW; X-ray; 2.90 A; Q=1-96.
DR PDB; 2OTJ; X-ray; 2.90 A; Q=1-96.
DR PDB; 2OTL; X-ray; 2.70 A; Q=1-96.
DR PDB; 2QA4; X-ray; 3.00 A; Q=1-96.
DR PDB; 2QEX; X-ray; 2.90 A; Q=1-96.
DR PDB; 3CC2; X-ray; 2.40 A; Q=1-96.
DR PDB; 3CC4; X-ray; 2.70 A; Q=1-96.
DR PDB; 3CC7; X-ray; 2.70 A; Q=1-96.
DR PDB; 3CCE; X-ray; 2.75 A; Q=1-96.
DR PDB; 3CCJ; X-ray; 2.70 A; Q=1-96.
DR PDB; 3CCL; X-ray; 2.90 A; Q=1-96.
DR PDB; 3CCM; X-ray; 2.55 A; Q=1-96.
DR PDB; 3CCQ; X-ray; 2.90 A; Q=1-96.
DR PDB; 3CCR; X-ray; 3.00 A; Q=1-96.
DR PDB; 3CCS; X-ray; 2.95 A; Q=1-96.
DR PDB; 3CCU; X-ray; 2.80 A; Q=1-96.
DR PDB; 3CCV; X-ray; 2.90 A; Q=1-96.
DR PDB; 3CD6; X-ray; 2.75 A; Q=1-96.
DR PDB; 3CMA; X-ray; 2.80 A; Q=1-96.
DR PDB; 3CME; X-ray; 2.95 A; Q=1-96.
DR PDB; 3CPW; X-ray; 2.70 A; P=1-96.
DR PDB; 3CXC; X-ray; 3.00 A; P=2-96.
DR PDB; 3G4S; X-ray; 3.20 A; Q=2-96.
DR PDB; 3G6E; X-ray; 2.70 A; Q=2-96.
DR PDB; 3G71; X-ray; 2.85 A; Q=2-96.
DR PDB; 3I55; X-ray; 3.11 A; Q=1-96.
DR PDB; 3I56; X-ray; 2.90 A; Q=1-96.
DR PDB; 3OW2; X-ray; 2.70 A; P=2-96.
DR PDB; 4ADX; EM; 6.60 A; Q=1-96.
DR PDB; 4V9F; X-ray; 2.40 A; Q=1-96.
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; P12734; -.
DR SMR; P12734; -.
DR IntAct; P12734; 2.
DR STRING; 272569.rrnAC0260; -.
DR EnsemblBacteria; AAV45317; AAV45317; rrnAC0260.
DR GeneID; 40154555; -.
DR GeneID; 64822986; -.
DR KEGG; hma:rrnAC0260; -.
DR PATRIC; fig|272569.17.peg.1055; -.
DR eggNOG; arCOG04129; Archaea.
DR HOGENOM; CLU_103610_1_1_2; -.
DR OMA; KGMPHRR; -.
DR EvolutionaryTrace; P12734; -.
DR Proteomes; UP000001169; Chromosome I.
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 Gene3D; 2.30.30.70; -; 1.
DR HAMAP; MF_00369; Ribosomal_L21e; 1.
DR InterPro; IPR036948; Ribosomal_L21_sf.
DR InterPro; IPR001147; Ribosomal_L21e.
DR InterPro; IPR022856; Ribosomal_L21e_arc.
DR InterPro; IPR018259; Ribosomal_L21e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR Pfam; PF01157; Ribosomal_L21e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01171; RIBOSOMAL_L21E; 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:3350019"
FT CHAIN 2..96
FT /note="50S ribosomal protein L21e"
FT /id="PRO_0000149686"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 96 AA; 10548 MW; DE6DE036844EF1F2 CRC64;
MPSSNGPLEG TRGKLKNKPR DRGTSPPQRA VEEFDDGEKV HLKIDPSVPN GRFHPRFDGQ
TGTVEGKQGD AYKVDIVDGG KEKTIIVTAA HLRRQE
