RL3_HALMA
ID RL3_HALMA Reviewed; 338 AA.
AC P20279; Q5V1S4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=50S ribosomal protein L3;
DE AltName: Full=Hl1;
DE AltName: Full=Hmal3;
GN Name=rpl3; OrderedLocusNames=rrnAC1611;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7;
RA Arndt E., Kroemer W., Hatakeyama T.;
RT "Organization and nucleotide sequence of a gene cluster coding for eight
RT ribosomal proteins in the archaebacterium Halobacterium marismortui.";
RL J. Biol. Chem. 265:3034-3039(1990).
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.
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: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L24e. Interacts weakly with protein L13.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000305}.
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DR EMBL; J05222; AAA86859.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46528.1; -; Genomic_DNA.
DR PIR; C35063; R5HS3L.
DR RefSeq; WP_004957423.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; B=2-338.
DR PDB; 1JJ2; X-ray; 2.40 A; B=2-338.
DR PDB; 1K73; X-ray; 3.01 A; D=2-338.
DR PDB; 1K8A; X-ray; 3.00 A; D=2-338.
DR PDB; 1K9M; X-ray; 3.00 A; D=2-338.
DR PDB; 1KC8; X-ray; 3.01 A; D=2-338.
DR PDB; 1KD1; X-ray; 3.00 A; D=2-338.
DR PDB; 1KQS; X-ray; 3.10 A; B=2-338.
DR PDB; 1M1K; X-ray; 3.20 A; D=2-338.
DR PDB; 1M90; X-ray; 2.80 A; D=2-338.
DR PDB; 1ML5; EM; 14.00 A; e=2-311, e=312-338.
DR PDB; 1N8R; X-ray; 3.00 A; D=2-338.
DR PDB; 1NJI; X-ray; 3.00 A; D=2-338.
DR PDB; 1Q7Y; X-ray; 3.20 A; D=2-338.
DR PDB; 1Q81; X-ray; 2.95 A; D=2-338.
DR PDB; 1Q82; X-ray; 2.98 A; D=2-338.
DR PDB; 1Q86; X-ray; 3.00 A; D=2-338.
DR PDB; 1QVF; X-ray; 3.10 A; B=2-338.
DR PDB; 1QVG; X-ray; 2.90 A; B=2-338.
DR PDB; 1S72; X-ray; 2.40 A; B=1-338.
DR PDB; 1VQ4; X-ray; 2.70 A; B=1-338.
DR PDB; 1VQ5; X-ray; 2.60 A; B=1-338.
DR PDB; 1VQ6; X-ray; 2.70 A; B=1-338.
DR PDB; 1VQ7; X-ray; 2.50 A; B=1-338.
DR PDB; 1VQ8; X-ray; 2.20 A; B=1-338.
DR PDB; 1VQ9; X-ray; 2.40 A; B=1-338.
DR PDB; 1VQK; X-ray; 2.30 A; B=1-338.
DR PDB; 1VQL; X-ray; 2.30 A; B=1-338.
DR PDB; 1VQM; X-ray; 2.30 A; B=1-338.
DR PDB; 1VQN; X-ray; 2.40 A; B=1-338.
DR PDB; 1VQO; X-ray; 2.20 A; B=1-338.
DR PDB; 1VQP; X-ray; 2.25 A; B=1-338.
DR PDB; 1W2B; X-ray; 3.50 A; B=2-338.
DR PDB; 1YHQ; X-ray; 2.40 A; B=1-338.
DR PDB; 1YI2; X-ray; 2.65 A; B=1-338.
DR PDB; 1YIJ; X-ray; 2.60 A; B=1-338.
DR PDB; 1YIT; X-ray; 2.80 A; B=1-338.
DR PDB; 1YJ9; X-ray; 2.90 A; B=1-338.
DR PDB; 1YJN; X-ray; 3.00 A; B=1-338.
DR PDB; 1YJW; X-ray; 2.90 A; B=1-338.
DR PDB; 2OTJ; X-ray; 2.90 A; B=1-338.
DR PDB; 2OTL; X-ray; 2.70 A; B=2-338.
DR PDB; 2QA4; X-ray; 3.00 A; B=1-338.
DR PDB; 2QEX; X-ray; 2.90 A; B=1-338.
DR PDB; 3CC2; X-ray; 2.40 A; B=1-338.
DR PDB; 3CC4; X-ray; 2.70 A; B=1-338.
DR PDB; 3CC7; X-ray; 2.70 A; B=1-338.
DR PDB; 3CCE; X-ray; 2.75 A; B=1-338.
DR PDB; 3CCJ; X-ray; 2.70 A; B=1-338.
DR PDB; 3CCL; X-ray; 2.90 A; B=1-338.
DR PDB; 3CCM; X-ray; 2.55 A; B=1-338.
DR PDB; 3CCQ; X-ray; 2.90 A; B=1-338.
DR PDB; 3CCR; X-ray; 3.00 A; B=1-338.
DR PDB; 3CCS; X-ray; 2.95 A; B=1-338.
DR PDB; 3CCU; X-ray; 2.80 A; B=1-338.
DR PDB; 3CCV; X-ray; 2.90 A; B=1-338.
DR PDB; 3CD6; X-ray; 2.75 A; B=1-338.
DR PDB; 3CMA; X-ray; 2.80 A; B=1-338.
DR PDB; 3CME; X-ray; 2.95 A; B=1-338.
DR PDB; 3CPW; X-ray; 2.70 A; B=1-338.
DR PDB; 3CXC; X-ray; 3.00 A; B=2-338.
DR PDB; 3G4S; X-ray; 3.20 A; B=2-338.
DR PDB; 3G6E; X-ray; 2.70 A; B=2-338.
DR PDB; 3G71; X-ray; 2.85 A; B=2-338.
DR PDB; 3I55; X-ray; 3.11 A; B=1-338.
DR PDB; 3I56; X-ray; 2.90 A; B=1-338.
DR PDB; 3OW2; X-ray; 2.70 A; B=2-338.
DR PDB; 4ADX; EM; 6.60 A; B=1-338.
DR PDB; 4V42; X-ray; 5.50 A; BE=2-338.
DR PDB; 4V4R; X-ray; 5.90 A; BE=2-338.
DR PDB; 4V4S; X-ray; 6.76 A; BE=2-338.
DR PDB; 4V4T; X-ray; 6.46 A; E=2-338.
DR PDB; 4V9F; X-ray; 2.40 A; B=1-338.
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; 1ML5; -.
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; 4V42; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P20279; -.
DR SMR; P20279; -.
DR IntAct; P20279; 3.
DR STRING; 272569.rrnAC1611; -.
DR EnsemblBacteria; AAV46528; AAV46528; rrnAC1611.
DR GeneID; 40152577; -.
DR GeneID; 64821815; -.
DR KEGG; hma:rrnAC1611; -.
DR PATRIC; fig|272569.17.peg.2301; -.
DR eggNOG; arCOG04070; Archaea.
DR HOGENOM; CLU_033361_2_0_2; -.
DR OMA; HQRTEYN; -.
DR EvolutionaryTrace; P20279; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F: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 Gene3D; 4.10.960.10; -; 1.
DR HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR InterPro; IPR045077; L3_arc_euk.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019928; Ribosomal_L3_arc.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11363; PTHR11363; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03626; L3_arch; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 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 CHAIN 2..338
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000077207"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 311
FT /note="R -> P (in Ref. 1; AAA86859)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="F -> FF (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1VQP"
FT STRAND 42..55
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3CCJ"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3CC4"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3CCR"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1VQK"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1YIJ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1VQK"
FT STRAND 262..279
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 338 AA; 37341 MW; 996D3BE503F4DBD4 CRC64;
MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT HVVLVNDEPN
SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE VWTDEFHSEL DRTLDVPEDH
DPDAAEEQIR DAHEAGDLGD LRLITHTVPD AVPSVPKKKP DVMETRVGGG SVSDRLDHAL
DIVEDGGEHA MNDIFRAGEY ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL
GPWNPSRVRS TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG
SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG
