ID E6J701_9ACTN Unreviewed; 131 AA.
AC E6J701;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ECO:0000313|EMBL:EFV92608.1};
GN ORFNames=ES5_04978 {ECO:0000313|EMBL:EFV92608.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV92608.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV92608.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV92608.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV92608.1}.
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DR EMBL; AEKG01000104; EFV92608.1; -; Genomic_DNA.
DR RefSeq; WP_007628102.1; NZ_AEKG01000104.1.
DR AlphaFoldDB; E6J701; -.
DR GeneID; 74898374; -.
DR Proteomes; UP000004165; 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 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}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 131 AA; 14201 MW; 46B4F21B6BC2EE1D CRC64;
MSSTKKRSPL GTDASTARRE GRARRHYRLR KKVSGTPERP RLVVNRSSRH IHAQIVDDLA
GRTLAAASTI EADVRSLEGD KKARSAKVGQ LLAERAKAAG IDAVVFDRGG NKYHGRIASL
ADAAREGGLE F
//