RL7A_PYRFU
ID RL7A_PYRFU Reviewed; 123 AA.
AC Q8U160;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE AltName: Full=Large ribosomal subunit protein eL8;
DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; OrderedLocusNames=PF1367;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEXES WITH FLPA NOP5 AND BOX
RP C/D RNA, AND SUBUNIT.
RX PubMed=20864039; DOI=10.1016/j.molcel.2010.08.022;
RA Xue S., Wang R., Yang F., Terns R.M., Terns M.P., Zhang X., Maxwell E.S.,
RA Li H.;
RT "Structural basis for substrate placement by an archaeal box C/D
RT ribonucleoprotein particle.";
RL Mol. Cell 39:939-949(2010).
RN [3] {ECO:0007744|PDB:4V6U}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.6 ANGSTROMS) OF 70S RIBOSOME, AND
RP SUBUNIT.
RX PubMed=23222135; DOI=10.1093/nar/gks1259;
RA Armache J.P., Anger A.M., Marquez V., Franckenberg S., Frohlich T.,
RA Villa E., Berninghausen O., Thomm M., Arnold G.J., Beckmann R.,
RA Wilson D.N.;
RT "Promiscuous behaviour of archaeal ribosomal proteins: implications for
RT eukaryotic ribosome evolution.";
RL Nucleic Acids Res. 41:1284-1293(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. Component of the 70S ribosome
CC (PubMed:23222135). Component of a box C/D small ribonucleoprotein
CC (sRNP) particle that is involved in pre-rRNA and tRNA processing.
CC Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-
CC specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA.
CC Site specificity is provided by a guide RNA that base pairs with the
CC substrate. Methylation occurs at a characteristic distance from the
CC sequence involved in base pairing with the guide RNA.
CC {ECO:0000269|PubMed:20864039, ECO:0000269|PubMed:23222135}.
CC -!- SUBUNIT: May be present in up to 3 copies per 70S ribosome
CC (PubMed:23222135). Part of the 50S ribosomal subunit, where it binds
CC 23S rRNA at its canonical site near the L1 stalk, as well as a possible
CC second 50S binding site near helix 25 and a possible third site on the
CC beak of the 30S subunit (PubMed:23222135). Component of box C/D small
CC ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5,
CC plus a guide RNA. These sRNP particles form homodimers, giving rise to
CC an asymmetric holoenzyme. Probably part of the RNase P complex
CC (PubMed:20864039). {ECO:0000269|PubMed:20864039,
CC ECO:0000269|PubMed:23222135}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAL81491.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE009950; AAL81491.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014835393.1; NZ_CP023154.1.
DR PDB; 2HVY; X-ray; 2.30 A; D=1-123.
DR PDB; 3HAX; X-ray; 2.11 A; D=2-123.
DR PDB; 3HAY; X-ray; 4.99 A; D=2-123.
DR PDB; 3HJW; X-ray; 2.35 A; C=3-122.
DR PDB; 3LWO; X-ray; 2.86 A; C=1-123.
DR PDB; 3LWP; X-ray; 2.50 A; C=1-123.
DR PDB; 3LWQ; X-ray; 2.68 A; C=1-123.
DR PDB; 3LWR; X-ray; 2.20 A; C=1-123.
DR PDB; 3LWV; X-ray; 2.50 A; C=1-123.
DR PDB; 3NMU; X-ray; 2.73 A; C/G=2-123.
DR PDB; 3NVI; X-ray; 2.71 A; B/D=2-123.
DR PDB; 3NVK; X-ray; 3.21 A; E/H=2-123.
DR PDB; 4BY9; NMR; -; D/G/J/M=3-123.
DR PDB; 4V4N; EM; 9.00 A; 3/G=1-123.
DR PDB; 4V6U; EM; 6.60 A; A3/B4/BG=1-123.
DR PDB; 5JB3; EM; 5.34 A; 3=1-123.
DR PDB; 5JBH; EM; 5.34 A; 3=1-123.
DR PDB; 6TPH; NMR; -; A=1-123.
DR PDB; 7OZQ; X-ray; 1.91 A; A/B/C/D=1-123.
DR PDBsum; 2HVY; -.
DR PDBsum; 3HAX; -.
DR PDBsum; 3HAY; -.
DR PDBsum; 3HJW; -.
DR PDBsum; 3LWO; -.
DR PDBsum; 3LWP; -.
DR PDBsum; 3LWQ; -.
DR PDBsum; 3LWR; -.
DR PDBsum; 3LWV; -.
DR PDBsum; 3NMU; -.
DR PDBsum; 3NVI; -.
DR PDBsum; 3NVK; -.
DR PDBsum; 4BY9; -.
DR PDBsum; 4V4N; -.
DR PDBsum; 4V6U; -.
DR PDBsum; 5JB3; -.
DR PDBsum; 5JBH; -.
DR PDBsum; 6TPH; -.
DR PDBsum; 7OZQ; -.
DR AlphaFoldDB; Q8U160; -.
DR BMRB; Q8U160; -.
DR SASBDB; Q8U160; -.
DR SMR; Q8U160; -.
DR DIP; DIP-48528N; -.
DR IntAct; Q8U160; 2.
DR STRING; 186497.PF1367; -.
DR EnsemblBacteria; AAL81491; AAL81491; PF1367.
DR GeneID; 41713171; -.
DR KEGG; pfu:PF1367; -.
DR PATRIC; fig|186497.12.peg.1430; -.
DR eggNOG; arCOG01751; Archaea.
DR HOGENOM; CLU_084513_4_0_2; -.
DR OMA; KPFYVRF; -.
DR OrthoDB; 114541at2157; -.
DR PhylomeDB; Q8U160; -.
DR EvolutionaryTrace; Q8U160; -.
DR Proteomes; UP000001013; Chromosome.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing.
FT CHAIN 1..123
FT /note="50S ribosomal protein L7Ae"
FT /id="PRO_0000136802"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:7OZQ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:7OZQ"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7OZQ"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:7OZQ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:7OZQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3NMU"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7OZQ"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:7OZQ"
SQ SEQUENCE 123 AA; 13395 MW; 934817F41BE2D4C5 CRC64;
MAKPSYVKFE VPKELAEKAL QAVEIARDTG KIRKGTNETT KAVERGQAKL VIIAEDVDPE
EIVAHLPPLC EEKEIPYIYV PSKKELGAAA GIEVAAASVA IIEPGKARDL VEEIAMKVKE
LMK
