RL31_HALMA
ID RL31_HALMA Reviewed; 92 AA.
AC P18138; Q5UY29;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=50S ribosomal protein L31e;
DE AltName: Full=Hl30;
DE AltName: Full=L34;
GN Name=rpl31e; OrderedLocusNames=rrnAC3113;
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=2207169; DOI=10.1016/0167-4781(90)90141-n;
RA Bergmann U., Arndt E.;
RT "Evidence for an additional archaebacterial gene cluster in Halobacterium
RT marismortui encoding ribosomal proteins HL46e and HL30.";
RL Biochim. Biophys. Acta 1050:56-60(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 2-92, AND ACETYLATION AT SER-2.
RX PubMed=2198942; DOI=10.1016/0167-4838(90)90269-l;
RA Hatakeyama T., Hatakeyama T.;
RT "Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the
RT archaebacterium Halobacterium marismortui.";
RL Biochim. Biophys. Acta 1039:343-347(1990).
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: Binds to the 23S rRNA. Located at the polypeptide exit tunnel
CC on the outside of the subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family.
CC {ECO:0000305}.
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DR EMBL; X55007; CAA38751.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV47824.1; -; Genomic_DNA.
DR PIR; S13067; R5HSER.
DR RefSeq; WP_004964660.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; U=2-92.
DR PDB; 1JJ2; X-ray; 2.40 A; W=2-92.
DR PDB; 1K73; X-ray; 3.01 A; Y=2-92.
DR PDB; 1K8A; X-ray; 3.00 A; Y=2-92.
DR PDB; 1K9M; X-ray; 3.00 A; Y=2-92.
DR PDB; 1KC8; X-ray; 3.01 A; Y=2-92.
DR PDB; 1KD1; X-ray; 3.00 A; Y=2-92.
DR PDB; 1KQS; X-ray; 3.10 A; W=2-92.
DR PDB; 1M1K; X-ray; 3.20 A; Y=2-92.
DR PDB; 1M90; X-ray; 2.80 A; Y=2-92.
DR PDB; 1N8R; X-ray; 3.00 A; Y=2-92.
DR PDB; 1NJI; X-ray; 3.00 A; Y=2-92.
DR PDB; 1Q7Y; X-ray; 3.20 A; Y=2-92.
DR PDB; 1Q81; X-ray; 2.95 A; Y=2-92.
DR PDB; 1Q82; X-ray; 2.98 A; Y=2-92.
DR PDB; 1Q86; X-ray; 3.00 A; Y=2-92.
DR PDB; 1QVF; X-ray; 3.10 A; W=2-92.
DR PDB; 1QVG; X-ray; 2.90 A; W=2-92.
DR PDB; 1S72; X-ray; 2.40 A; X=1-92.
DR PDB; 1VQ4; X-ray; 2.70 A; X=1-92.
DR PDB; 1VQ5; X-ray; 2.60 A; X=1-92.
DR PDB; 1VQ6; X-ray; 2.70 A; X=1-92.
DR PDB; 1VQ7; X-ray; 2.50 A; X=1-92.
DR PDB; 1VQ8; X-ray; 2.20 A; X=1-92.
DR PDB; 1VQ9; X-ray; 2.40 A; X=1-92.
DR PDB; 1VQK; X-ray; 2.30 A; X=1-92.
DR PDB; 1VQL; X-ray; 2.30 A; X=1-92.
DR PDB; 1VQM; X-ray; 2.30 A; X=1-92.
DR PDB; 1VQN; X-ray; 2.40 A; X=1-92.
DR PDB; 1VQO; X-ray; 2.20 A; X=1-92.
DR PDB; 1VQP; X-ray; 2.25 A; X=1-92.
DR PDB; 1W2B; X-ray; 3.50 A; W=2-92.
DR PDB; 1YHQ; X-ray; 2.40 A; X=1-92.
DR PDB; 1YI2; X-ray; 2.65 A; X=1-92.
DR PDB; 1YIJ; X-ray; 2.60 A; X=1-92.
DR PDB; 1YIT; X-ray; 2.80 A; X=1-92.
DR PDB; 1YJ9; X-ray; 2.90 A; X=1-92.
DR PDB; 1YJN; X-ray; 3.00 A; X=1-92.
DR PDB; 1YJW; X-ray; 2.90 A; X=1-92.
DR PDB; 2OTJ; X-ray; 2.90 A; X=1-92.
DR PDB; 2OTL; X-ray; 2.70 A; X=1-92.
DR PDB; 2QA4; X-ray; 3.00 A; X=1-92.
DR PDB; 2QEX; X-ray; 2.90 A; X=1-92.
DR PDB; 3CC2; X-ray; 2.40 A; X=1-92.
DR PDB; 3CC4; X-ray; 2.70 A; X=1-92.
DR PDB; 3CC7; X-ray; 2.70 A; X=1-92.
DR PDB; 3CCE; X-ray; 2.75 A; X=1-92.
DR PDB; 3CCJ; X-ray; 2.70 A; X=1-92.
DR PDB; 3CCL; X-ray; 2.90 A; X=1-92.
DR PDB; 3CCM; X-ray; 2.55 A; X=1-92.
DR PDB; 3CCQ; X-ray; 2.90 A; X=1-92.
DR PDB; 3CCR; X-ray; 3.00 A; X=1-92.
DR PDB; 3CCS; X-ray; 2.95 A; X=1-92.
DR PDB; 3CCU; X-ray; 2.80 A; X=1-92.
DR PDB; 3CCV; X-ray; 2.90 A; X=1-92.
DR PDB; 3CD6; X-ray; 2.75 A; X=1-92.
DR PDB; 3CMA; X-ray; 2.80 A; X=1-92.
DR PDB; 3CME; X-ray; 2.95 A; X=1-92.
DR PDB; 3CPW; X-ray; 2.70 A; W=1-92.
DR PDB; 3CXC; X-ray; 3.00 A; W=2-92.
DR PDB; 3G4S; X-ray; 3.20 A; X=8-89.
DR PDB; 3G6E; X-ray; 2.70 A; X=8-89.
DR PDB; 3G71; X-ray; 2.85 A; X=8-89.
DR PDB; 3I55; X-ray; 3.11 A; X=1-92.
DR PDB; 3I56; X-ray; 2.90 A; X=1-92.
DR PDB; 3OW2; X-ray; 2.70 A; W=8-89.
DR PDB; 4ADX; EM; 6.60 A; X=1-92.
DR PDB; 4V9F; X-ray; 2.40 A; X=1-92.
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; P18138; -.
DR SMR; P18138; -.
DR IntAct; P18138; 2.
DR STRING; 272569.rrnAC3113; -.
DR iPTMnet; P18138; -.
DR PRIDE; P18138; -.
DR EnsemblBacteria; AAV47824; AAV47824; rrnAC3113.
DR GeneID; 40153924; -.
DR GeneID; 64823661; -.
DR KEGG; hma:rrnAC3113; -.
DR PATRIC; fig|272569.17.peg.3655; -.
DR eggNOG; arCOG04473; Archaea.
DR HOGENOM; CLU_112570_3_2_2; -.
DR OMA; MEERIYT; -.
DR EvolutionaryTrace; P18138; -.
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 CDD; cd00463; Ribosomal_L31e; 1.
DR Gene3D; 3.10.440.10; -; 1.
DR HAMAP; MF_00410; Ribosomal_L31e; 1.
DR InterPro; IPR000054; Ribosomal_L31e.
DR InterPro; IPR020052; Ribosomal_L31e_CS.
DR InterPro; IPR023621; Ribosomal_L31e_dom_sf.
DR PANTHER; PTHR10956; PTHR10956; 1.
DR Pfam; PF01198; Ribosomal_L31e; 1.
DR SMART; SM01380; Ribosomal_L31e; 1.
DR SUPFAM; SSF54575; SSF54575; 1.
DR PROSITE; PS01144; RIBOSOMAL_L31E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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:2198942"
FT CHAIN 2..92
FT /note="50S ribosomal protein L31e"
FT /id="PRO_0000153791"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2198942"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1VQM"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 92 AA; 10367 MW; 0FF505E03E8F6C4A CRC64;
MSASDFEERV VTIPLRDARA EPNHKRADKA MILIREHLAK HFSVDEDAVR LDPSINEAAW
ARGRANTPSK IRVRAARFEE EGEAIVEAET AE
