ID   RL7A_AERPE              Reviewed;         127 AA.
AC   Q9YAX7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE   AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN   Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; OrderedLocusNames=APE_1818;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 4-127.
RX   PubMed=23989144; DOI=10.1107/s1744309113021799;
RA   Bhuiya M.W., Suryadi J., Zhou Z., Brown B.A. II;
RT   "Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight
RT   into its extreme thermostability.";
RL   Acta Crystallogr. F 69:979-988(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:0000255|HAMAP-Rule:MF_00326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Probably part of the RNase
CC       P complex. {ECO:0000255|HAMAP-Rule:MF_00326}.
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}.
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DR   EMBL; BA000002; BAA80821.1; -; Genomic_DNA.
DR   PIR; H72566; H72566.
DR   PDB; 2FC3; X-ray; 1.56 A; A=4-127.
DR   PDBsum; 2FC3; -.
DR   AlphaFoldDB; Q9YAX7; -.
DR   SMR; Q9YAX7; -.
DR   STRING; 272557.APE_1818; -.
DR   EnsemblBacteria; BAA80821; BAA80821; APE_1818.
DR   KEGG; ape:APE_1818; -.
DR   PATRIC; fig|272557.25.peg.1219; -.
DR   eggNOG; arCOG01751; Archaea.
DR   OMA; KPFYVRF; -.
DR   EvolutionaryTrace; Q9YAX7; -.
DR   Proteomes; UP000002518; 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: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; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; tRNA processing.
FT   CHAIN           1..127
FT                   /note="50S ribosomal protein L7Ae"
FT                   /id="PRO_0000136788"
FT   HELIX           13..29
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           36..44
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           66..72
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           83..89
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:2FC3"
FT   HELIX           108..125
FT                   /evidence="ECO:0007829|PDB:2FC3"
SQ   SEQUENCE   127 AA;  13952 MW;  21BF3E1A072BB8E6 CRC64;
     MSKPIYVRFE VPEDLAEKAY EAVKRARETG RIKKGTNETT KAVERGLAKL VVIAEDVDPP
     EIVMHLPLLC DEKKIPYVYV PSKKRLGEAA GIEVAAASVA IIEPGDAETL VREIVEKVKE
     LRAKAGV