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Database: UniProt
Entry: A0A1F8KYD4_9CHLR
LinkDB: A0A1F8KYD4_9CHLR
Original site: A0A1F8KYD4_9CHLR 
ID   A0A1F8KYD4_9CHLR        Unreviewed;       115 AA.
AC   A0A1F8KYD4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-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=A2082_07015 {ECO:0000313|EMBL:OGN78826.1};
OS   Chloroflexi bacterium GWC2_70_10.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797615 {ECO:0000313|EMBL:OGN78826.1, ECO:0000313|Proteomes:UP000180316};
RN   [1] {ECO:0000313|EMBL:OGN78826.1, ECO:0000313|Proteomes:UP000180316}
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:OGN78826.1}.
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DR   EMBL; MGMI01000102; OGN78826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8KYD4; -.
DR   Proteomes; UP000180316; 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   115 AA;  12554 MW;  62A8573A6039E75C CRC64;
     MPADTRREGR LMRHRRVRKR VAGTGERPRL AVFRSLSHIY AQVIDDRAGR TVAAASDVGA
     KAGNKTERAK LVGKALADKA RAAGVAEVVF DRGGYRYHGR VKALADAARE AGLRF
//
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