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RL37_HALMA
ID   RL37_HALMA              Reviewed;          57 AA.
AC   P32410;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=50S ribosomal protein L37e;
DE   AltName: Full=L35e;
GN   Name=rpl37e; OrderedLocusNames=rrnAC0797.1;
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 2-57.
RX   PubMed=8504167; DOI=10.1016/0167-4781(93)90181-c;
RA   Bergmann U., Wittmann-Liebold B.;
RT   "HL35e and HLA: primary structure of two very basic and cysteine-rich
RT   ribosomal proteins from Haloarcula marismortui.";
RL   Biochim. Biophys. Acta 1173:195-200(1993).
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   -!- FUNCTION: Binds to the 23S rRNA.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC       protein L4. {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC       {ECO:0000305}.
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DR   EMBL; AY596297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S33789; S33789.
DR   RefSeq; WP_004517916.1; NZ_CP039138.1.
DR   PDB; 1FFK; X-ray; 2.40 A; X=2-57.
DR   PDB; 1JJ2; X-ray; 2.40 A; Z=2-57.
DR   PDB; 1K73; X-ray; 3.01 A; 2=2-57.
DR   PDB; 1K8A; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1K9M; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1KC8; X-ray; 3.01 A; 2=2-57.
DR   PDB; 1KD1; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1KQS; X-ray; 3.10 A; Z=2-57.
DR   PDB; 1M1K; X-ray; 3.20 A; 2=2-57.
DR   PDB; 1M90; X-ray; 2.80 A; 2=2-57.
DR   PDB; 1N8R; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1NJI; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1Q7Y; X-ray; 3.20 A; 2=2-57.
DR   PDB; 1Q81; X-ray; 2.95 A; 2=2-57.
DR   PDB; 1Q82; X-ray; 2.98 A; 2=2-57.
DR   PDB; 1Q86; X-ray; 3.00 A; 2=2-57.
DR   PDB; 1QVF; X-ray; 3.10 A; Z=2-57.
DR   PDB; 1QVG; X-ray; 2.90 A; Z=2-57.
DR   PDB; 1S72; X-ray; 2.40 A; 1=1-57.
DR   PDB; 1VQ4; X-ray; 2.70 A; 1=1-57.
DR   PDB; 1VQ5; X-ray; 2.60 A; 1=1-57.
DR   PDB; 1VQ6; X-ray; 2.70 A; 1=1-57.
DR   PDB; 1VQ7; X-ray; 2.50 A; 1=1-57.
DR   PDB; 1VQ8; X-ray; 2.20 A; 1=1-57.
DR   PDB; 1VQ9; X-ray; 2.40 A; 1=1-57.
DR   PDB; 1VQK; X-ray; 2.30 A; 1=1-57.
DR   PDB; 1VQL; X-ray; 2.30 A; 1=1-57.
DR   PDB; 1VQM; X-ray; 2.30 A; 1=1-57.
DR   PDB; 1VQN; X-ray; 2.40 A; 1=1-57.
DR   PDB; 1VQO; X-ray; 2.20 A; 1=1-57.
DR   PDB; 1VQP; X-ray; 2.25 A; 1=1-57.
DR   PDB; 1W2B; X-ray; 3.50 A; Z=2-57.
DR   PDB; 1YHQ; X-ray; 2.40 A; 1=1-57.
DR   PDB; 1YI2; X-ray; 2.65 A; 1=1-57.
DR   PDB; 1YIJ; X-ray; 2.60 A; 1=1-57.
DR   PDB; 1YIT; X-ray; 2.80 A; 1=1-57.
DR   PDB; 1YJ9; X-ray; 2.90 A; 1=1-57.
DR   PDB; 1YJN; X-ray; 3.00 A; 1=1-57.
DR   PDB; 1YJW; X-ray; 2.90 A; 1=1-57.
DR   PDB; 2OTJ; X-ray; 2.90 A; 1=1-57.
DR   PDB; 2OTL; X-ray; 2.70 A; 1=1-57.
DR   PDB; 2QA4; X-ray; 3.00 A; 1=1-57.
DR   PDB; 2QEX; X-ray; 2.90 A; 1=1-57.
DR   PDB; 3CC2; X-ray; 2.40 A; 1=1-57.
DR   PDB; 3CC4; X-ray; 2.70 A; 1=1-57.
DR   PDB; 3CC7; X-ray; 2.70 A; 1=1-57.
DR   PDB; 3CCE; X-ray; 2.75 A; 1=1-57.
DR   PDB; 3CCJ; X-ray; 2.70 A; 1=1-57.
DR   PDB; 3CCL; X-ray; 2.90 A; 1=1-57.
DR   PDB; 3CCM; X-ray; 2.55 A; 1=1-57.
DR   PDB; 3CCQ; X-ray; 2.90 A; 1=1-57.
DR   PDB; 3CCR; X-ray; 3.00 A; 1=1-57.
DR   PDB; 3CCS; X-ray; 2.95 A; 1=1-57.
DR   PDB; 3CCU; X-ray; 2.80 A; 1=1-57.
DR   PDB; 3CCV; X-ray; 2.90 A; 1=1-57.
DR   PDB; 3CD6; X-ray; 2.75 A; 1=1-57.
DR   PDB; 3CMA; X-ray; 2.80 A; 1=1-57.
DR   PDB; 3CME; X-ray; 2.95 A; 1=1-57.
DR   PDB; 3CPW; X-ray; 2.70 A; Z=1-57.
DR   PDB; 3CXC; X-ray; 3.00 A; Z=2-57.
DR   PDB; 3G4S; X-ray; 3.20 A; 1=2-57.
DR   PDB; 3G6E; X-ray; 2.70 A; 1=2-57.
DR   PDB; 3G71; X-ray; 2.85 A; 1=2-57.
DR   PDB; 3I55; X-ray; 3.11 A; 1=1-57.
DR   PDB; 3I56; X-ray; 2.90 A; 1=1-57.
DR   PDB; 3OW2; X-ray; 2.70 A; Z=2-57.
DR   PDB; 4ADX; EM; 6.60 A; 1=1-57.
DR   PDB; 4V9F; X-ray; 2.40 A; 1=1-57.
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; P32410; -.
DR   SMR; P32410; -.
DR   IntAct; P32410; 2.
DR   GeneID; 44857407; -.
DR   GeneID; 64822544; -.
DR   EvolutionaryTrace; P32410; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.20.25.30; -; 1.
DR   HAMAP; MF_00547; Ribosomal_L37e; 1.
DR   InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR   InterPro; IPR001569; Ribosomal_L37e.
DR   InterPro; IPR018267; Ribosomal_L37e_CS.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   Pfam; PF01907; Ribosomal_L37e; 1.
DR   SUPFAM; SSF57829; SSF57829; 1.
DR   PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Metal-binding; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8504167"
FT   CHAIN           2..57
FT                   /note="50S ribosomal protein L37e"
FT                   /id="PRO_0000139726"
FT   ZN_FING         20..38
FT                   /note="C4-type"
FT                   /evidence="ECO:0000305"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            30..33
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:1VQ8"
SQ   SEQUENCE   57 AA;  6314 MW;  A21A05AACA3112EC CRC64;
     MTGAGTPSQG KKNTTTHTKC RRCGEKSYHT KKKVCSSCGF GKSAKRRDYE WQSKAGE
 
 
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