RL44E_HALMA
ID RL44E_HALMA Reviewed; 92 AA.
AC P32411; Q5UX20;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=50S ribosomal protein L44e {ECO:0000255|HAMAP-Rule:MF_01476};
DE AltName: Full=HLA;
DE AltName: Full=La;
GN Name=rpl44e {ECO:0000255|HAMAP-Rule:MF_01476}; OrderedLocusNames=rrnAC3514;
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 PROTEIN SEQUENCE, AND SUBUNIT.
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 [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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT, SUBUNIT,
RP RRNA-BINDING, AND PROBABLE COFACTOR.
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, RRNA-BINDING, AND TRNA-BINDING.
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. Binds deacetylated tRNA in the E site;
CC when the tRNA binds a stretch of 7 amino acids are displaced to allow
CC binding.
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 L15e. Binds the E site tRNA. {ECO:0000255|HAMAP-Rule:MF_01476,
CC ECO:0000269|PubMed:10937989, ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128, ECO:0000269|PubMed:8504167}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000255|HAMAP-Rule:MF_01476}.
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DR EMBL; AY596297; AAV48183.1; -; Genomic_DNA.
DR PIR; S33790; S33790.
DR RefSeq; WP_004593654.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; Z=1-92.
DR PDB; 1JJ2; X-ray; 2.40 A; 2=1-92.
DR PDB; 1K73; X-ray; 3.01 A; 4=1-92.
DR PDB; 1K8A; X-ray; 3.00 A; 4=1-92.
DR PDB; 1K9M; X-ray; 3.00 A; 4=1-92.
DR PDB; 1KC8; X-ray; 3.01 A; 4=1-92.
DR PDB; 1KD1; X-ray; 3.00 A; 4=1-92.
DR PDB; 1KQS; X-ray; 3.10 A; 2=1-92.
DR PDB; 1M1K; X-ray; 3.20 A; 4=1-92.
DR PDB; 1M90; X-ray; 2.80 A; 4=1-92.
DR PDB; 1N8R; X-ray; 3.00 A; 4=1-92.
DR PDB; 1NJI; X-ray; 3.00 A; 4=1-92.
DR PDB; 1Q7Y; X-ray; 3.20 A; 4=1-92.
DR PDB; 1Q81; X-ray; 2.95 A; 4=1-92.
DR PDB; 1Q82; X-ray; 2.98 A; 4=1-92.
DR PDB; 1Q86; X-ray; 3.00 A; 4=1-92.
DR PDB; 1QVF; X-ray; 3.10 A; 2=1-92.
DR PDB; 1QVG; X-ray; 2.90 A; 2=1-92.
DR PDB; 1S72; X-ray; 2.40 A; 3=1-92.
DR PDB; 1VQ4; X-ray; 2.70 A; 3=1-92.
DR PDB; 1VQ5; X-ray; 2.60 A; 3=1-92.
DR PDB; 1VQ6; X-ray; 2.70 A; 3=1-92.
DR PDB; 1VQ7; X-ray; 2.50 A; 3=1-92.
DR PDB; 1VQ8; X-ray; 2.20 A; 3=1-92.
DR PDB; 1VQ9; X-ray; 2.40 A; 3=1-92.
DR PDB; 1VQK; X-ray; 2.30 A; 3=1-92.
DR PDB; 1VQL; X-ray; 2.30 A; 3=1-92.
DR PDB; 1VQM; X-ray; 2.30 A; 3=1-92.
DR PDB; 1VQN; X-ray; 2.40 A; 3=1-92.
DR PDB; 1VQO; X-ray; 2.20 A; 3=1-92.
DR PDB; 1VQP; X-ray; 2.25 A; 3=1-92.
DR PDB; 1W2B; X-ray; 3.50 A; 2=1-92.
DR PDB; 1YHQ; X-ray; 2.40 A; 3=1-92.
DR PDB; 1YI2; X-ray; 2.65 A; 3=1-92.
DR PDB; 1YIJ; X-ray; 2.60 A; 3=1-92.
DR PDB; 1YIT; X-ray; 2.80 A; 3=1-92.
DR PDB; 1YJ9; X-ray; 2.90 A; 3=1-92.
DR PDB; 1YJN; X-ray; 3.00 A; 3=1-92.
DR PDB; 1YJW; X-ray; 2.90 A; 3=1-92.
DR PDB; 2OTJ; X-ray; 2.90 A; 3=1-92.
DR PDB; 2OTL; X-ray; 2.70 A; 3=1-92.
DR PDB; 2QA4; X-ray; 3.00 A; 3=1-92.
DR PDB; 2QEX; X-ray; 2.90 A; 3=1-92.
DR PDB; 3CC2; X-ray; 2.40 A; 3=1-92.
DR PDB; 3CC4; X-ray; 2.70 A; 3=1-92.
DR PDB; 3CC7; X-ray; 2.70 A; 3=1-92.
DR PDB; 3CCE; X-ray; 2.75 A; 3=1-92.
DR PDB; 3CCJ; X-ray; 2.70 A; 3=1-92.
DR PDB; 3CCL; X-ray; 2.90 A; 3=1-92.
DR PDB; 3CCM; X-ray; 2.55 A; 3=1-92.
DR PDB; 3CCQ; X-ray; 2.90 A; 3=1-92.
DR PDB; 3CCR; X-ray; 3.00 A; 3=1-92.
DR PDB; 3CCS; X-ray; 2.95 A; 3=1-92.
DR PDB; 3CCU; X-ray; 2.80 A; 3=1-92.
DR PDB; 3CCV; X-ray; 2.90 A; 3=1-92.
DR PDB; 3CD6; X-ray; 2.75 A; 3=1-92.
DR PDB; 3CMA; X-ray; 2.80 A; 3=1-92.
DR PDB; 3CME; X-ray; 2.95 A; 3=1-92.
DR PDB; 3CPW; X-ray; 2.70 A; 2=1-92.
DR PDB; 3CXC; X-ray; 3.00 A; 2=1-92.
DR PDB; 3G4S; X-ray; 3.20 A; 3=1-92.
DR PDB; 3G6E; X-ray; 2.70 A; 3=1-92.
DR PDB; 3G71; X-ray; 2.85 A; 3=1-92.
DR PDB; 3I55; X-ray; 3.11 A; 3=1-92.
DR PDB; 3I56; X-ray; 2.90 A; 3=1-92.
DR PDB; 3OW2; X-ray; 2.70 A; 2=1-92.
DR PDB; 4ADX; EM; 6.60 A; 3=1-92.
DR PDB; 4V9F; X-ray; 2.40 A; 3=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; P32411; -.
DR SMR; P32411; -.
DR IntAct; P32411; 2.
DR STRING; 272569.rrnAC3514; -.
DR PRIDE; P32411; -.
DR EnsemblBacteria; AAV48183; AAV48183; rrnAC3514.
DR GeneID; 40154285; -.
DR GeneID; 64823264; -.
DR KEGG; hma:rrnAC3514; -.
DR PATRIC; fig|272569.17.peg.4020; -.
DR eggNOG; arCOG04109; Archaea.
DR HOGENOM; CLU_114645_3_0_2; -.
DR OMA; CKKHTIH; -.
DR EvolutionaryTrace; P32411; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01476; Ribosomal_L44e; 1.
DR InterPro; IPR000552; Ribosomal_L44e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 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;
KW tRNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..92
FT /note="50S ribosomal protein L44e"
FT /id="PRO_0000149150"
FT ZN_FING 11..74
FT /note="C4-type"
FT /evidence="ECO:0000305"
FT REGION 22..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3CCR"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3I55"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3CCS"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1VQP"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 92 AA; 10791 MW; 14197AA6AE7AC07A CRC64;
MQMPRRFNTY CPHCNEHQEH EVEKVRSGRQ TGMKWIDRQR ERNSGIGNDG KFSKVPGGDK
PTKKTDLKYR CGECGKAHLR EGWRAGRLEF QE
