ID A0A1F6EIH8_9BACT Unreviewed; 116 AA.
AC A0A1F6EIH8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
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=A3A34_02395 {ECO:0000313|EMBL:OGG73428.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_50_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798507 {ECO:0000313|EMBL:OGG73428.1, ECO:0000313|Proteomes:UP000178587};
RN [1] {ECO:0000313|EMBL:OGG73428.1, ECO:0000313|Proteomes:UP000178587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG73428.1}.
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DR EMBL; MFLU01000019; OGG73428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6EIH8; -.
DR STRING; 1798507.A3A34_02395; -.
DR Proteomes; UP000178587; 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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 116 AA; 12839 MW; C162A08C8409FD67 CRC64;
MKTNTSKIQQ RTRRHRRVRA KVSGTAVRPR LSVYKSNMRF VAQIIDDERG QTLAAVSSSK
EKGKTPQERA ESAAKTLAKQ AHEKGVESVV FDRGGFKYTG TVKAFADAAR AAGLRF
//