RL15E_HALMA
ID RL15E_HALMA Reviewed; 196 AA.
AC P60618; P12740; Q5V0N3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=50S ribosomal protein L15e;
DE AltName: Full=50S ribosomal protein LC12;
GN Name=rpl15e; OrderedLocusNames=rrnAC2065;
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 2-21.
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 [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 -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein L7Ae
CC and weakly with L44e. {ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family.
CC {ECO:0000305}.
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DR EMBL; AY596297; AAV46920.1; -; Genomic_DNA.
DR PIR; H28949; H28949.
DR RefSeq; WP_004958369.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; I=37-194.
DR PDB; 1JJ2; X-ray; 2.40 A; L=2-194.
DR PDB; 1K73; X-ray; 3.01 A; N=2-194.
DR PDB; 1K8A; X-ray; 3.00 A; N=2-194.
DR PDB; 1K9M; X-ray; 3.00 A; N=2-194.
DR PDB; 1KC8; X-ray; 3.01 A; N=2-194.
DR PDB; 1KD1; X-ray; 3.00 A; N=2-194.
DR PDB; 1KQS; X-ray; 3.10 A; L=2-194.
DR PDB; 1M1K; X-ray; 3.20 A; N=2-194.
DR PDB; 1M90; X-ray; 2.80 A; N=2-194.
DR PDB; 1N8R; X-ray; 3.00 A; N=2-194.
DR PDB; 1NJI; X-ray; 3.00 A; N=2-194.
DR PDB; 1Q7Y; X-ray; 3.20 A; N=2-194.
DR PDB; 1Q81; X-ray; 2.95 A; N=2-194.
DR PDB; 1Q82; X-ray; 2.98 A; N=2-194.
DR PDB; 1Q86; X-ray; 3.00 A; N=2-194.
DR PDB; 1QVF; X-ray; 3.10 A; L=2-194.
DR PDB; 1QVG; X-ray; 2.90 A; L=2-194.
DR PDB; 1S72; X-ray; 2.40 A; M=2-194.
DR PDB; 1VQ4; X-ray; 2.70 A; M=2-194.
DR PDB; 1VQ5; X-ray; 2.60 A; M=2-194.
DR PDB; 1VQ6; X-ray; 2.70 A; M=2-194.
DR PDB; 1VQ7; X-ray; 2.50 A; M=2-194.
DR PDB; 1VQ8; X-ray; 2.20 A; M=2-194.
DR PDB; 1VQ9; X-ray; 2.40 A; M=1-194.
DR PDB; 1VQK; X-ray; 2.30 A; M=1-194.
DR PDB; 1VQL; X-ray; 2.30 A; M=1-194.
DR PDB; 1VQM; X-ray; 2.30 A; M=1-194.
DR PDB; 1VQN; X-ray; 2.40 A; M=2-194.
DR PDB; 1VQO; X-ray; 2.20 A; M=1-194.
DR PDB; 1VQP; X-ray; 2.25 A; M=1-194.
DR PDB; 1W2B; X-ray; 3.50 A; L=2-194.
DR PDB; 1YHQ; X-ray; 2.40 A; M=2-195.
DR PDB; 1YI2; X-ray; 2.65 A; M=1-195.
DR PDB; 1YIJ; X-ray; 2.60 A; M=1-195.
DR PDB; 1YIT; X-ray; 2.80 A; M=1-195.
DR PDB; 1YJ9; X-ray; 2.90 A; M=1-195.
DR PDB; 1YJN; X-ray; 3.00 A; M=1-195.
DR PDB; 1YJW; X-ray; 2.90 A; M=1-195.
DR PDB; 2OTJ; X-ray; 2.90 A; M=2-194.
DR PDB; 2OTL; X-ray; 2.70 A; M=2-194.
DR PDB; 2QA4; X-ray; 3.00 A; M=1-194.
DR PDB; 2QEX; X-ray; 2.90 A; M=1-194.
DR PDB; 3CC2; X-ray; 2.40 A; M=1-196.
DR PDB; 3CC4; X-ray; 2.70 A; M=1-196.
DR PDB; 3CC7; X-ray; 2.70 A; M=1-196.
DR PDB; 3CCE; X-ray; 2.75 A; M=1-196.
DR PDB; 3CCJ; X-ray; 2.70 A; M=1-196.
DR PDB; 3CCL; X-ray; 2.90 A; M=1-196.
DR PDB; 3CCM; X-ray; 2.55 A; M=1-196.
DR PDB; 3CCQ; X-ray; 2.90 A; M=1-196.
DR PDB; 3CCR; X-ray; 3.00 A; M=1-196.
DR PDB; 3CCS; X-ray; 2.95 A; M=1-196.
DR PDB; 3CCU; X-ray; 2.80 A; M=1-196.
DR PDB; 3CCV; X-ray; 2.90 A; M=1-196.
DR PDB; 3CD6; X-ray; 2.75 A; M=1-196.
DR PDB; 3CMA; X-ray; 2.80 A; M=1-196.
DR PDB; 3CME; X-ray; 2.95 A; M=1-196.
DR PDB; 3CPW; X-ray; 2.70 A; L=1-196.
DR PDB; 3G4S; X-ray; 3.20 A; M=2-195.
DR PDB; 3G6E; X-ray; 2.70 A; M=2-195.
DR PDB; 3G71; X-ray; 2.85 A; M=2-195.
DR PDB; 3I55; X-ray; 3.11 A; M=2-194.
DR PDB; 3I56; X-ray; 2.90 A; M=2-194.
DR PDB; 4ADX; EM; 6.60 A; M=1-196.
DR PDB; 4V9F; X-ray; 2.40 A; M=1-196.
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; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P60618; -.
DR SMR; P60618; -.
DR IntAct; P60618; 2.
DR STRING; 272569.rrnAC2065; -.
DR EnsemblBacteria; AAV46920; AAV46920; rrnAC2065.
DR GeneID; 40152982; -.
DR GeneID; 64821404; -.
DR KEGG; hma:rrnAC2065; -.
DR PATRIC; fig|272569.17.peg.2714; -.
DR eggNOG; arCOG04209; Archaea.
DR HOGENOM; CLU_080796_1_0_2; -.
DR OMA; KYMQELY; -.
DR EvolutionaryTrace; P60618; -.
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; 3.40.1120.10; -; 1.
DR HAMAP; MF_00256; Ribosomal_L15e; 1.
DR InterPro; IPR024794; Rbsml_L15e_core_dom_sf.
DR InterPro; IPR000439; Ribosomal_L15e.
DR InterPro; IPR020926; Ribosomal_L15e_arc.
DR InterPro; IPR020925; Ribosomal_L15e_CS.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR PANTHER; PTHR11847; PTHR11847; 1.
DR Pfam; PF00827; Ribosomal_L15e; 1.
DR SMART; SM01384; Ribosomal_L15e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS01194; RIBOSOMAL_L15E; 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:3196689"
FT CHAIN 2..196
FT /note="50S ribosomal protein L15e"
FT /id="PRO_0000127570"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 13
FT /note="W -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3CC4"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 188..192
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 196 AA; 22355 MW; 502449E0A6BC23BB CRC64;
MARSAYSYIR DAWKNPGDGQ LAELQWQRQQ EWRNEGAVER IERPTRLDKA RSQGYKAKQG
VIVARVSVRK GSARKRRHKA GRRSKRQGVT RITRRKDIQR VAEERASRTF PNLRVLNSYS
VGQDGRQKWH EVILIDPNHP AIQNDDDLSW ICADDQADRV FRGLTGAGRR NRGLSGKGKG
SEKTRPSLRS NGGKGK
