RL19E_HALMA
ID RL19E_HALMA Reviewed; 149 AA.
AC P14119; Q5V1U0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=50S ribosomal protein L19e {ECO:0000255|HAMAP-Rule:MF_01475};
DE AltName: Full=Hl24;
DE AltName: Full=Hmal19;
GN Name=rpl19e {ECO:0000255|HAMAP-Rule:MF_01475}; OrderedLocusNames=rrnAC1594;
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=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 [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 2-149, AND SUBUNIT.
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 [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. {ECO:0000255|HAMAP-
CC Rule:MF_01475, ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128, ECO:0000269|PubMed:2591382}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000255|HAMAP-Rule:MF_01475}.
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DR EMBL; X58395; CAA41289.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46512.1; -; Genomic_DNA.
DR PIR; S16540; R5HSH4.
DR RefSeq; WP_004516953.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; M=2-149.
DR PDB; 1JJ2; X-ray; 2.40 A; O=2-149.
DR PDB; 1K73; X-ray; 3.01 A; Q=2-149.
DR PDB; 1K8A; X-ray; 3.00 A; Q=2-149.
DR PDB; 1K9M; X-ray; 3.00 A; Q=2-149.
DR PDB; 1KC8; X-ray; 3.01 A; Q=2-149.
DR PDB; 1KD1; X-ray; 3.00 A; Q=2-149.
DR PDB; 1KQS; X-ray; 3.10 A; O=2-149.
DR PDB; 1M1K; X-ray; 3.20 A; Q=2-149.
DR PDB; 1M90; X-ray; 2.80 A; Q=2-149.
DR PDB; 1N8R; X-ray; 3.00 A; Q=2-149.
DR PDB; 1NJI; X-ray; 3.00 A; Q=2-149.
DR PDB; 1Q7Y; X-ray; 3.20 A; Q=2-149.
DR PDB; 1Q81; X-ray; 2.95 A; Q=2-149.
DR PDB; 1Q82; X-ray; 2.98 A; Q=2-149.
DR PDB; 1Q86; X-ray; 3.00 A; Q=2-149.
DR PDB; 1QVF; X-ray; 3.10 A; O=2-149.
DR PDB; 1QVG; X-ray; 2.90 A; O=2-149.
DR PDB; 1S72; X-ray; 2.40 A; P=1-149.
DR PDB; 1VQ4; X-ray; 2.70 A; P=1-149.
DR PDB; 1VQ5; X-ray; 2.60 A; P=1-149.
DR PDB; 1VQ6; X-ray; 2.70 A; P=1-149.
DR PDB; 1VQ7; X-ray; 2.50 A; P=1-149.
DR PDB; 1VQ8; X-ray; 2.20 A; P=1-149.
DR PDB; 1VQ9; X-ray; 2.40 A; P=1-149.
DR PDB; 1VQK; X-ray; 2.30 A; P=1-149.
DR PDB; 1VQL; X-ray; 2.30 A; P=1-149.
DR PDB; 1VQM; X-ray; 2.30 A; P=1-149.
DR PDB; 1VQN; X-ray; 2.40 A; P=1-149.
DR PDB; 1VQO; X-ray; 2.20 A; P=1-149.
DR PDB; 1VQP; X-ray; 2.25 A; P=1-149.
DR PDB; 1W2B; X-ray; 3.50 A; O=2-149.
DR PDB; 1YHQ; X-ray; 2.40 A; P=1-149.
DR PDB; 1YI2; X-ray; 2.65 A; P=1-149.
DR PDB; 1YIJ; X-ray; 2.60 A; P=1-149.
DR PDB; 1YIT; X-ray; 2.80 A; P=1-149.
DR PDB; 1YJ9; X-ray; 2.90 A; P=1-149.
DR PDB; 1YJN; X-ray; 3.00 A; P=1-149.
DR PDB; 1YJW; X-ray; 2.90 A; P=1-149.
DR PDB; 2OTJ; X-ray; 2.90 A; P=1-149.
DR PDB; 2OTL; X-ray; 2.70 A; P=1-149.
DR PDB; 2QA4; X-ray; 3.00 A; P=1-149.
DR PDB; 2QEX; X-ray; 2.90 A; P=1-149.
DR PDB; 3CC2; X-ray; 2.40 A; P=1-149.
DR PDB; 3CC4; X-ray; 2.70 A; P=1-149.
DR PDB; 3CC7; X-ray; 2.70 A; P=1-149.
DR PDB; 3CCE; X-ray; 2.75 A; P=1-149.
DR PDB; 3CCJ; X-ray; 2.70 A; P=1-149.
DR PDB; 3CCL; X-ray; 2.90 A; P=1-149.
DR PDB; 3CCM; X-ray; 2.55 A; P=1-149.
DR PDB; 3CCQ; X-ray; 2.90 A; P=1-149.
DR PDB; 3CCR; X-ray; 3.00 A; P=1-149.
DR PDB; 3CCS; X-ray; 2.95 A; P=1-149.
DR PDB; 3CCU; X-ray; 2.80 A; P=1-149.
DR PDB; 3CCV; X-ray; 2.90 A; P=1-149.
DR PDB; 3CD6; X-ray; 2.75 A; P=1-149.
DR PDB; 3CMA; X-ray; 2.80 A; P=1-149.
DR PDB; 3CME; X-ray; 2.95 A; P=1-149.
DR PDB; 3CPW; X-ray; 2.70 A; O=1-149.
DR PDB; 3CXC; X-ray; 3.00 A; O=2-149.
DR PDB; 3G4S; X-ray; 3.20 A; P=2-144.
DR PDB; 3G6E; X-ray; 2.70 A; P=2-144.
DR PDB; 3G71; X-ray; 2.85 A; P=2-144.
DR PDB; 3I55; X-ray; 3.11 A; P=1-149.
DR PDB; 3I56; X-ray; 2.90 A; P=1-149.
DR PDB; 3OW2; X-ray; 2.70 A; O=2-144.
DR PDB; 4ADX; EM; 6.60 A; P=1-149.
DR PDB; 4V9F; X-ray; 2.40 A; P=1-149.
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; P14119; -.
DR SMR; P14119; -.
DR IntAct; P14119; 2.
DR STRING; 272569.rrnAC1594; -.
DR EnsemblBacteria; AAV46512; AAV46512; rrnAC1594.
DR GeneID; 40152559; -.
DR GeneID; 64821833; -.
DR KEGG; hma:rrnAC1594; -.
DR PATRIC; fig|272569.17.peg.2283; -.
DR eggNOG; arCOG04089; Archaea.
DR HOGENOM; CLU_083919_1_1_2; -.
DR OMA; NRVWIDP; -.
DR EvolutionaryTrace; P14119; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd01418; Ribosomal_L19e_A; 1.
DR Gene3D; 1.10.1200.60; -; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR Gene3D; 1.20.5.560; -; 1.
DR HAMAP; MF_01475; Ribosomal_L19e; 1.
DR InterPro; IPR035970; 60S_ribosomal_L19/L19e_sf.
DR InterPro; IPR000196; Ribosomal_L19/L19e.
DR InterPro; IPR023638; Ribosomal_L19/L19e_CS.
DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1.
DR InterPro; IPR033936; Ribosomal_L19e_A.
DR InterPro; IPR015973; Ribosomal_L19e_dom2.
DR InterPro; IPR015974; Ribosomal_L19e_dom3.
DR InterPro; IPR039547; RPL19.
DR PANTHER; PTHR10722; PTHR10722; 1.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SMART; SM01416; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; SSF48140; 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 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:2591382"
FT CHAIN 2..149
FT /note="50S ribosomal protein L19e"
FT /id="PRO_0000131187"
FT REGION 45..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 82
FT /note="K -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1VQ7"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 149 AA; 16762 MW; 210F99E836B0B817 CRC64;
MTDLSAQKRL AADVLDVGKN RVWFNPERQG DIADAITRED VRELVDEGAI QAKDKKGNSR
GRARERQKKR AYGHQKGAGS RKGKAGARQN SKEDWESRIR AQRTKLRELR DEGTLSSSQY
RDLYDKAGGG EFDSVADLER YIDANHGDA
