ID A0A1F7H2L1_9BACT Unreviewed; 120 AA.
AC A0A1F7H2L1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 15.
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=A3C25_03515 {ECO:0000313|EMBL:OGK25096.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPHIGHO2_02_FULL_38_11.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802039 {ECO:0000313|EMBL:OGK25096.1, ECO:0000313|Proteomes:UP000177913};
RN [1] {ECO:0000313|EMBL:OGK25096.1, ECO:0000313|Proteomes:UP000177913}
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:OGK25096.1}.
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DR EMBL; MFZO01000019; OGK25096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7H2L1; -.
DR Proteomes; UP000177913; 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}.
SQ SEQUENCE 120 AA; 13566 MW; D3AE7B74EEAF60B4 CRC64;
MGKISKNREI RRKKRISANI FGTREKPRIS AFSSNRYIYA QVIDDNNRIT IVSYSSLKLA
QAKNYNRGKK VEEAKKVGVE LAKKAVEKGI TQAVFDRGKY SYKGRVKALA EGLREGGLKI
//