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Database: UniProt
Entry: A0A117RML2_9ACTN
LinkDB: A0A117RML2_9ACTN
Original site: A0A117RML2_9ACTN 
ID   A0A117RML2_9ACTN        Unreviewed;       127 AA.
AC   A0A117RML2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000256|ARBA:ARBA00035197, ECO:0000256|HAMAP-Rule:MF_01337};
GN   Name=rplR {ECO:0000256|HAMAP-Rule:MF_01337};
GN   ORFNames=AQJ67_26170 {ECO:0000313|EMBL:KUN99120.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUN99120.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUN99120.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUN99120.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is one of the proteins that bind and probably mediate
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. {ECO:0000256|HAMAP-
CC       Rule:MF_01337}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01337}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000256|ARBA:ARBA00007116, ECO:0000256|HAMAP-Rule:MF_01337}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUN99120.1}.
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DR   EMBL; LMWY01000034; KUN99120.1; -; Genomic_DNA.
DR   RefSeq; WP_007494754.1; NZ_KQ948932.1.
DR   AlphaFoldDB; A0A117RML2; -.
DR   STRING; 661399.AQJ67_26170; -.
DR   OrthoDB; 9810939at2; -.
DR   Proteomes; UP000053429; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00432; Ribosomal_L18_L5e; 1.
DR   Gene3D; 3.30.420.100; -; 1.
DR   HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR   InterPro; IPR005484; Ribosomal_uL18.
DR   InterPro; IPR004389; Ribosomal_uL18_bac-type.
DR   NCBIfam; TIGR00060; L18_bact; 1.
DR   PANTHER; PTHR12899; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12899:SF3; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR   Pfam; PF00861; Ribosomal_L18p; 1.
DR   SUPFAM; SSF53137; Translational machinery components; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053429};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01337};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01337};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01337};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01337}.
SQ   SEQUENCE   127 AA;  13615 MW;  715712A6B6E45978 CRC64;
     MAYGQKILKG DAYKRAAIKR RHIRIRKHIN GTAERPRLVV TRSNRHIVAQ VIDDIKGHTL
     ASASTLDTSI RGGEGDKSAQ AKQVGALVAE RAKAAGVEAV VFDRGGNQYA GRIAALADAA
     REAGLKF
//
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