RL37A_HALMA
ID RL37A_HALMA Reviewed; 92 AA.
AC P60619; Q5V1M1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=50S ribosomal protein L37Ae {ECO:0000255|HAMAP-Rule:MF_00327};
DE AltName: Full=Ribosomal protein L43e {ECO:0000255|HAMAP-Rule:MF_00327};
GN Name=rpl37ae {ECO:0000255|HAMAP-Rule:MF_00327};
GN OrderedLocusNames=rrnAC1669;
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 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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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. Contacts protein L2.
CC {ECO:0000255|HAMAP-Rule:MF_00327, ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family.
CC Putative zinc-binding subfamily. {ECO:0000255|HAMAP-Rule:MF_00327}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV46581.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV46581.1; ALT_INIT; Genomic_DNA.
DR PDB; 1FFK; X-ray; 2.40 A; W=12-19.
DR PDB; 1JJ2; X-ray; 2.40 A; Y=49-79.
DR PDB; 1K73; X-ray; 3.01 A; 1=49-79.
DR PDB; 1K8A; X-ray; 3.00 A; 1=49-79.
DR PDB; 1K9M; X-ray; 3.00 A; 1=49-79.
DR PDB; 1KC8; X-ray; 3.01 A; 1=49-79.
DR PDB; 1KD1; X-ray; 3.00 A; 1=49-79.
DR PDB; 1KQS; X-ray; 3.10 A; Y=49-79.
DR PDB; 1M1K; X-ray; 3.20 A; 1=49-79.
DR PDB; 1M90; X-ray; 2.80 A; 1=49-79.
DR PDB; 1N8R; X-ray; 3.00 A; 1=49-79.
DR PDB; 1NJI; X-ray; 3.00 A; 1=49-79.
DR PDB; 1Q7Y; X-ray; 3.20 A; 1=49-79.
DR PDB; 1Q81; X-ray; 2.95 A; 1=49-79.
DR PDB; 1Q82; X-ray; 2.98 A; 1=49-79.
DR PDB; 1Q86; X-ray; 3.00 A; 1=49-79.
DR PDB; 1QVF; X-ray; 3.10 A; Y=49-79.
DR PDB; 1QVG; X-ray; 2.90 A; Y=49-79.
DR PDB; 1S72; X-ray; 2.40 A; Z=11-82.
DR PDB; 1VQ4; X-ray; 2.70 A; Z=11-92.
DR PDB; 1VQ5; X-ray; 2.60 A; Z=11-92.
DR PDB; 1VQ6; X-ray; 2.70 A; Z=11-92.
DR PDB; 1VQ7; X-ray; 2.50 A; Z=11-92.
DR PDB; 1VQ8; X-ray; 2.20 A; Z=11-92.
DR PDB; 1VQ9; X-ray; 2.40 A; Z=11-92.
DR PDB; 1VQK; X-ray; 2.30 A; Z=11-92.
DR PDB; 1VQL; X-ray; 2.30 A; Z=11-92.
DR PDB; 1VQM; X-ray; 2.30 A; Z=11-92.
DR PDB; 1VQN; X-ray; 2.40 A; Z=11-92.
DR PDB; 1VQO; X-ray; 2.20 A; Z=11-92.
DR PDB; 1VQP; X-ray; 2.25 A; Z=11-92.
DR PDB; 1W2B; X-ray; 3.50 A; Y=49-79.
DR PDB; 1YHQ; X-ray; 2.40 A; Z=11-92.
DR PDB; 1YI2; X-ray; 2.65 A; Z=11-92.
DR PDB; 1YIJ; X-ray; 2.60 A; Z=11-92.
DR PDB; 1YIT; X-ray; 2.80 A; Z=11-92.
DR PDB; 1YJ9; X-ray; 2.90 A; Z=11-92.
DR PDB; 1YJN; X-ray; 3.00 A; Z=11-92.
DR PDB; 1YJW; X-ray; 2.90 A; Z=11-92.
DR PDB; 2OTJ; X-ray; 2.90 A; Z=11-82.
DR PDB; 2OTL; X-ray; 2.70 A; Z=11-82.
DR PDB; 2QA4; X-ray; 3.00 A; Z=1-92.
DR PDB; 2QEX; X-ray; 2.90 A; Z=11-82.
DR PDB; 3CC2; X-ray; 2.40 A; Z=1-92.
DR PDB; 3CC4; X-ray; 2.70 A; Z=1-92.
DR PDB; 3CC7; X-ray; 2.70 A; Z=1-92.
DR PDB; 3CCE; X-ray; 2.75 A; Z=1-92.
DR PDB; 3CCJ; X-ray; 2.70 A; Z=1-92.
DR PDB; 3CCL; X-ray; 2.90 A; Z=1-92.
DR PDB; 3CCM; X-ray; 2.55 A; Z=1-92.
DR PDB; 3CCQ; X-ray; 2.90 A; Z=1-92.
DR PDB; 3CCR; X-ray; 3.00 A; Z=1-92.
DR PDB; 3CCS; X-ray; 2.95 A; Z=1-92.
DR PDB; 3CCU; X-ray; 2.80 A; Z=1-92.
DR PDB; 3CCV; X-ray; 2.90 A; Z=1-92.
DR PDB; 3CD6; X-ray; 2.75 A; Z=1-92.
DR PDB; 3CMA; X-ray; 2.80 A; Z=1-92.
DR PDB; 3CME; X-ray; 2.95 A; Z=1-92.
DR PDB; 3CPW; X-ray; 2.70 A; Y=1-92.
DR PDB; 3G4S; X-ray; 3.20 A; Z=10-82.
DR PDB; 3G6E; X-ray; 2.70 A; Z=10-82.
DR PDB; 3G71; X-ray; 2.85 A; Z=10-82.
DR PDB; 3I55; X-ray; 3.11 A; Z=1-92.
DR PDB; 3I56; X-ray; 2.90 A; Z=1-92.
DR PDB; 4ADX; EM; 6.60 A; Z=1-92.
DR PDB; 4V9F; X-ray; 2.40 A; Z=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; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P60619; -.
DR SMR; P60619; -.
DR IntAct; P60619; 2.
DR STRING; 272569.rrnAC1669; -.
DR EnsemblBacteria; AAV46581; AAV46581; rrnAC1669.
DR KEGG; hma:rrnAC1669; -.
DR PATRIC; fig|272569.17.peg.2356; -.
DR eggNOG; arCOG04208; Archaea.
DR HOGENOM; CLU_141199_2_0_2; -.
DR EvolutionaryTrace; P60619; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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: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_00327; Ribosomal_L37Ae; 1.
DR InterPro; IPR002674; Ribosomal_L37ae.
DR InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01780; Ribosomal_L37ae; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR TIGRFAMs; TIGR00280; eL43_euk_arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..92
FT /note="50S ribosomal protein L37Ae"
FT /id="PRO_0000139841"
FT ZN_FING 39..60
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00327"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00327"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00327"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00327"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00327"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3CCJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 92 AA; 10172 MW; 89E52AFE761E9837 CRC64;
MASKSGKTGS SGRFGARYGR VSRRRVAEIE SEMNEDHACP NCGEDRVDRQ GTGIWQCSYC
DYKFTGGSYK PETPGGKTVR RSIRAALSED EE
