ID   RL7A_SACS2              Reviewed;         127 AA.
AC   P55858;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Large ribosomal subunit protein eL8 {ECO:0000255|HAMAP-Rule:MF_00326, ECO:0000312|EMBL:CAA69560.1};
DE   AltName: Full=50S ribosomal protein L7Ae {ECO:0000303|PubMed:39753558};
DE   AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
DE   AltName: Full=Small ribosomal subunit protein eS12 {ECO:0000303|PubMed:39753558};
GN   Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326,
GN   ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0091;
GN   ORFNames=C04_031 {ECO:0000303|PubMed:8899719};
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1] {ECO:0000312|EMBL:CAA69560.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [3]
RP   SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=19036786; DOI=10.1093/nar/gkn959;
RA   Benelli D., Marzi S., Mancone C., Alonzi T., la Teana A., Londei P.;
RT   "Function and ribosomal localization of aIF6, a translational regulator
RT   shared by archaea and eukarya.";
RL   Nucleic Acids Res. 37:256-267(2009).
RN   [4]
RP   POSITION IN SMALL RIBOSOMAL SUBUNIT.
RA   Leibundgut M.A.;
RL   Unpublished observations (OCT-2025).
RN   [5] {ECO:0007744|PDB:3ID5}
RP   X-RAY CRYSTALLOGRAPHY (4.01 ANGSTROMS) IN COMPLEX WITH RNA; S-NOP5 AND
RP   FLPA, AND SUBUNIT.
RX   PubMed=19666563; DOI=10.1073/pnas.0905128106;
RA   Ye K., Jia R., Lin J., Ju M., Peng J., Xu A., Zhang L.;
RT   "Structural organization of box C/D RNA-guided RNA methyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:13808-13813(2009).
RN   [6] {ECO:0007744|PDB:9FHL, ECO:0007744|PDB:9FRA, ECO:0007744|PDB:9FRK, ECO:0007744|PDB:9FRL, ECO:0007744|PDB:9FS6, ECO:0007744|PDB:9FS8, ECO:0007744|PDB:9FSF, ECO:0007744|PDB:9FY0}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF RIBOSOMAL 30S
RP   INITIATION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=39753558; DOI=10.1038/s41467-024-55718-5;
RA   Bourgeois G., Coureux P.D., Lazennec-Schurdevin C., Madru C., Gaillard T.,
RA   Duchateau M., Chamot-Rooke J., Bourcier S., Mechulam Y., Schmitt E.;
RT   "Structures of Saccharolobus solfataricus initiation complexes with
RT   leaderless mRNAs highlight archaeal features and eukaryotic proximity.";
RL   Nat. Commun. 16:348-348(2025).
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 (PubMed:19666563) and box C'/D' sRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00326, ECO:0000269|PubMed:19666563}.
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:39753558).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:39753558). Binds 16S (small)
CC       rRNA (PubMed:39753558). {ECO:0000269|PubMed:39753558}.
CC   -!- SUBUNIT: Part of the 30 (PubMed:19036786, PubMed:39753558) and 50S
CC       (PubMed:19036786) ribosomal subunit. Component of box C/D small
CC       ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5,
CC       plus a guide RNA (PubMed:19666563). These sRNP particles form
CC       homodimers, giving rise to an asymmetric holoenzyme (PubMed:19666563).
CC       Probably part of the RNase P complex (By similarity).
CC       {ECO:0000250|UniProtKB:P62426, ECO:0000269|PubMed:19036786,
CC       ECO:0000269|PubMed:19666563, ECO:0000269|PubMed:39753558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326,
CC       ECO:0000269|PubMed:19036786}. Note=Found free in the cytoplasm and
CC       associated with 30S (PubMed:19036786, PubMed:39753558) and 50S
CC       (PubMed:19036786) ribosomal subunits (PubMed:19036786).
CC       {ECO:0000269|PubMed:19036786, ECO:0000269|PubMed:39753558}.
CC   -!- INDUCTION: Constitutuively expressed (at protein level).
CC       {ECO:0000269|PubMed:19036786}.
CC   -!- MISCELLANEOUS: In the small ribosomal subunit it is present at the
CC       position usually occupied by ribosomal protein eS12.
CC       {ECO:0000269|PubMed:39753558, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00326}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40449.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA69560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y08257; CAA69560.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE006641; AAK40449.1; ALT_INIT; Genomic_DNA.
DR   PIR; S75397; S75397.
DR   RefSeq; WP_009988903.1; NC_002754.1.
DR   PDB; 3ID5; X-ray; 4.01 A; C/G=1-127.
DR   PDB; 5GIN; X-ray; 3.31 A; C/D/L=3-127.
DR   PDB; 5GIO; X-ray; 3.60 A; C/D/L=3-127.
DR   PDB; 5GIP; X-ray; 3.13 A; C/D/M/N=3-127.
DR   PDB; 5JPQ; EM; 7.30 A; U/V=1-127.
DR   PDB; 9FHL; EM; 2.50 A; 3=1-127.
DR   PDB; 9FRA; EM; 2.80 A; 3=1-127.
DR   PDB; 9FRK; EM; 3.00 A; 3=1-127.
DR   PDB; 9FRL; EM; 2.97 A; 3=1-127.
DR   PDB; 9FS6; EM; 2.90 A; 3=1-127.
DR   PDB; 9FS8; EM; 3.70 A; 3=1-127.
DR   PDB; 9FSF; EM; 2.80 A; 3=1-127.
DR   PDB; 9FY0; EM; 2.90 A; 3=1-127.
DR   AlphaFoldDB; P55858; -.
DR   EMDB; EMD-50445; -.
DR   EMDB; EMD-50709; -.
DR   EMDB; EMD-50716; -.
DR   EMDB; EMD-50717; -.
DR   EMDB; EMD-50724; -.
DR   EMDB; EMD-50725; -.
DR   EMDB; EMD-50727; -.
DR   EMDB; EMD-50854; -.
DR   SMR; P55858; -.
DR   DIP; DIP-48940N; -.
DR   FunCoup; P55858; 231.
DR   IntAct; P55858; 1.
DR   STRING; 273057.SSO0091; -.
DR   PaxDb; 273057-SSO0091; -.
DR   EnsemblBacteria; AAK40449; AAK40449; SSO0091.
DR   GeneID; 42362205; -.
DR   GeneID; 44129051; -.
DR   KEGG; sso:SSO0091; -.
DR   PATRIC; fig|273057.12.peg.89; -.
DR   eggNOG; arCOG01751; Archaea.
DR   HOGENOM; CLU_084513_4_0_2; -.
DR   InParanoid; P55858; -.
DR   PhylomeDB; P55858; -.
DR   EvolutionaryTrace; P55858; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
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   FunFam; 3.30.1330.30:FF:000020; 50S ribosomal protein L7Ae; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   HAMAP; MF_00326; Ribosomal_eL8; 1.
DR   InterPro; IPR050257; eL8/uL1-like.
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; PTHR23105; RIBOSOMAL PROTEIN L7AE FAMILY MEMBER; 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.
DR   PDBsum; 3ID5; -.
DR   PDBsum; 5GIN; -.
DR   PDBsum; 5GIO; -.
DR   PDBsum; 5GIP; -.
DR   PDBsum; 5JPQ; -.
DR   PDBsum; 9FHL; -.
DR   PDBsum; 9FRA; -.
DR   PDBsum; 9FRK; -.
DR   PDBsum; 9FRL; -.
DR   PDBsum; 9FS6; -.
DR   PDBsum; 9FS8; -.
DR   PDBsum; 9FSF; -.
DR   PDBsum; 9FY0; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; tRNA processing.
FT   CHAIN           1..127
FT                   /note="Large ribosomal subunit protein eL8"
FT                   /id="PRO_0000136806"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:5GIP"
FT   HELIX           14..29
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   HELIX           37..45
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   HELIX           66..70
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:5GIP"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   TURN            108..112
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   HELIX           113..119
FT                   /evidence="ECO:0007829|PDB:9FHL"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:5GIN"
SQ   SEQUENCE   127 AA;  13736 MW;  3EE30FC81C1A003D CRC64;
     MSKASYVKFE VPQDLADKVL EAVRKAKESG KIKKGTNETT KAVERGQAKL VIIAEDVQPE
     EIVAHLPLLC DEKKIPYVYV SSKKALGEAC GLQVATASAA ILEPGEAKDL VDEIIKRVNE
     IKGKTSS
//