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   27-MAR-2024, entry version 128.
DE   RecName: Full=Large ribosomal subunit protein eL8 {ECO:0000255|HAMAP-Rule:MF_00326};
DE   AltName: Full=50S ribosomal protein L7Ae;
DE   AltName: Full=Ribosomal protein L8e;
GN   Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326};
GN   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   EMDB; EMD-8148; -.
DR   EMDB; EMD-8149; -.
DR   SASBDB; Q8U160; -.
DR   SMR; Q8U160; -.
DR   DIP; DIP-48528N; -.
DR   IntAct; Q8U160; 2.
DR   STRING; 186497.PF1367; -.
DR   PaxDb; 186497-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   OrthoDB; 25810at2157; -.
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:UniProtKB-KW.
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_eL8; 1.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004037; Ribosomal_eL8-like_CS.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   InterPro; IPR018492; Ribosomal_eL8/Nhp2.
DR   InterPro; IPR022481; Ribosomal_eL8_arc.
DR   NCBIfam; TIGR03677; eL8_ribo; 1.
DR   PANTHER; PTHR11843; 40S RIBOSOMAL PROTEIN S12; 1.
DR   PANTHER; PTHR11843:SF0; 40S RIBOSOMAL PROTEIN S12; 1.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   PRINTS; PR00881; L7ARS6FAMILY.
DR   PRINTS; PR00884; RIBOSOMALHS6.
DR   SUPFAM; SSF55315; L30e-like; 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="Large ribosomal subunit protein eL8"
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
//