RL7A_HALMA
ID RL7A_HALMA Reviewed; 120 AA.
AC P12743; Q5V5M3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE AltName: Full=Hs6;
DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; OrderedLocusNames=rrnAC0103;
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 2-120.
RX PubMed=3315748; DOI=10.1016/0014-5793(87)80423-4;
RA Kimura J., Arndt E., Kimura M.;
RT "Primary structures of three highly acidic ribosomal proteins S6, S12 and
RT S15 from the archaebacterium Halobacterium marismortui.";
RL FEBS Lett. 224:65-70(1987).
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: Multifunctional RNA-binding protein that recognizes the K-
CC turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA,
CC box C/D and box C'/D' sRNAs. {ECO:0000305}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein
CC L15e. Probably part of the RNase P complex.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000255|HAMAP-Rule:MF_00326}.
CC -!- CAUTION: Was originally thought to be a protein from the small subunit
CC of the ribosome. {ECO:0000305|PubMed:3315748}.
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DR EMBL; AY596297; AAV45179.1; -; Genomic_DNA.
DR PIR; S00182; R5HSS6.
DR RefSeq; WP_004593501.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; E=2-120.
DR PDB; 1JJ2; X-ray; 2.40 A; F=2-120.
DR PDB; 1K73; X-ray; 3.01 A; H=2-120.
DR PDB; 1K8A; X-ray; 3.00 A; H=2-120.
DR PDB; 1K9M; X-ray; 3.00 A; H=2-120.
DR PDB; 1KC8; X-ray; 3.01 A; H=2-120.
DR PDB; 1KD1; X-ray; 3.00 A; H=2-120.
DR PDB; 1KQS; X-ray; 3.10 A; F=2-120.
DR PDB; 1M1K; X-ray; 3.20 A; H=2-120.
DR PDB; 1M90; X-ray; 2.80 A; H=2-120.
DR PDB; 1N8R; X-ray; 3.00 A; H=2-120.
DR PDB; 1NJI; X-ray; 3.00 A; H=2-120.
DR PDB; 1Q7Y; X-ray; 3.20 A; H=2-120.
DR PDB; 1Q81; X-ray; 2.95 A; H=2-120.
DR PDB; 1Q82; X-ray; 2.98 A; H=2-120.
DR PDB; 1Q86; X-ray; 3.00 A; H=2-120.
DR PDB; 1QVF; X-ray; 3.10 A; F=2-120.
DR PDB; 1QVG; X-ray; 2.90 A; F=2-120.
DR PDB; 1S72; X-ray; 2.40 A; F=1-120.
DR PDB; 1VQ4; X-ray; 2.70 A; F=1-120.
DR PDB; 1VQ5; X-ray; 2.60 A; F=1-120.
DR PDB; 1VQ6; X-ray; 2.70 A; F=1-120.
DR PDB; 1VQ7; X-ray; 2.50 A; F=1-120.
DR PDB; 1VQ8; X-ray; 2.20 A; F=1-120.
DR PDB; 1VQ9; X-ray; 2.40 A; F=1-120.
DR PDB; 1VQK; X-ray; 2.30 A; F=1-120.
DR PDB; 1VQL; X-ray; 2.30 A; F=1-120.
DR PDB; 1VQM; X-ray; 2.30 A; F=1-120.
DR PDB; 1VQN; X-ray; 2.40 A; F=1-120.
DR PDB; 1VQO; X-ray; 2.20 A; F=1-120.
DR PDB; 1VQP; X-ray; 2.25 A; F=1-120.
DR PDB; 1W2B; X-ray; 3.50 A; F=2-120.
DR PDB; 1YHQ; X-ray; 2.40 A; F=1-120.
DR PDB; 1YI2; X-ray; 2.65 A; F=1-120.
DR PDB; 1YIJ; X-ray; 2.60 A; F=1-120.
DR PDB; 1YIT; X-ray; 2.80 A; F=1-120.
DR PDB; 1YJ9; X-ray; 2.90 A; F=1-120.
DR PDB; 1YJN; X-ray; 3.00 A; F=1-120.
DR PDB; 1YJW; X-ray; 2.90 A; F=1-120.
DR PDB; 2OTJ; X-ray; 2.90 A; F=1-120.
DR PDB; 2OTL; X-ray; 2.70 A; F=1-120.
DR PDB; 2QA4; X-ray; 3.00 A; F=1-120.
DR PDB; 2QEX; X-ray; 2.90 A; F=1-120.
DR PDB; 3CC2; X-ray; 2.40 A; F=1-120.
DR PDB; 3CC4; X-ray; 2.70 A; F=1-120.
DR PDB; 3CC7; X-ray; 2.70 A; F=1-120.
DR PDB; 3CCE; X-ray; 2.75 A; F=1-120.
DR PDB; 3CCJ; X-ray; 2.70 A; F=1-120.
DR PDB; 3CCL; X-ray; 2.90 A; F=1-120.
DR PDB; 3CCM; X-ray; 2.55 A; F=1-120.
DR PDB; 3CCQ; X-ray; 2.90 A; F=1-120.
DR PDB; 3CCR; X-ray; 3.00 A; F=1-120.
DR PDB; 3CCS; X-ray; 2.95 A; F=1-120.
DR PDB; 3CCU; X-ray; 2.80 A; F=1-120.
DR PDB; 3CCV; X-ray; 2.90 A; F=1-120.
DR PDB; 3CD6; X-ray; 2.75 A; F=1-120.
DR PDB; 3CMA; X-ray; 2.80 A; F=1-120.
DR PDB; 3CME; X-ray; 2.95 A; F=1-120.
DR PDB; 3CPW; X-ray; 2.70 A; F=1-120.
DR PDB; 3CXC; X-ray; 3.00 A; F=2-120.
DR PDB; 3G4S; X-ray; 3.20 A; F=2-120.
DR PDB; 3G6E; X-ray; 2.70 A; F=2-120.
DR PDB; 3G71; X-ray; 2.85 A; F=2-120.
DR PDB; 3I55; X-ray; 3.11 A; F=1-120.
DR PDB; 3I56; X-ray; 2.90 A; F=1-120.
DR PDB; 3OW2; X-ray; 2.70 A; F=2-120.
DR PDB; 4ADX; EM; 6.60 A; F=1-120.
DR PDB; 4V9F; X-ray; 2.40 A; F=1-120.
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; P12743; -.
DR SMR; P12743; -.
DR IntAct; P12743; 2.
DR STRING; 272569.rrnAC0103; -.
DR EnsemblBacteria; AAV45179; AAV45179; rrnAC0103.
DR GeneID; 40154413; -.
DR GeneID; 64823135; -.
DR KEGG; hma:rrnAC0103; -.
DR PATRIC; fig|272569.17.peg.907; -.
DR eggNOG; arCOG01751; Archaea.
DR HOGENOM; CLU_084513_4_0_2; -.
DR OMA; KPFYVRF; -.
DR EvolutionaryTrace; P12743; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.30; -; 1.
DR HAMAP; MF_00326; Ribosomal_L7Ae_Arch; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR022481; Ribosomal_L7Ae_arc.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR InterPro; IPR000948; Ribosomal_L7Ae_prok.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00884; RIBOSOMALHS6.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR03677; eL8_ribo; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3315748"
FT CHAIN 2..120
FT /note="50S ribosomal protein L7Ae"
FT /id="PRO_0000136790"
FT CONFLICT 104..111
FT /note="EADADVED -> AAATV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1VQO"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 120 AA; 12782 MW; 96132F5CB51840A0 CRC64;
MPVYVDFDVP ADLEDDALEA LEVARDTGAV KKGTNETTKS IERGSAELVF VAEDVQPEEI
VMHIPELADE KGVPFIFVEQ QDDLGHAAGL EVGSAAAAVT DAGEADADVE DIADKVEELR
