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Database: UniProt
Entry: M2ZGL1_9NOCA
LinkDB: M2ZGL1_9NOCA
Original site: M2ZGL1_9NOCA 
ID   M2ZGL1_9NOCA            Unreviewed;       135 AA.
AC   M2ZGL1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:EME59469.1};
GN   ORFNames=G352_20048 {ECO:0000313|EMBL:EME59469.1};
OS   Rhodococcus ruber BKS 20-38.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1278076 {ECO:0000313|EMBL:EME59469.1, ECO:0000313|Proteomes:UP000011731};
RN   [1] {ECO:0000313|EMBL:EME59469.1, ECO:0000313|Proteomes:UP000011731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BKS 20-38 {ECO:0000313|EMBL:EME59469.1,
RC   ECO:0000313|Proteomes:UP000011731};
RX   PubMed=23558535;
RA   Bala M., Kumar S., Raghava G.P., Mayilraj S.;
RT   "Draft Genome Sequence of Rhodococcus ruber Strain BKS 20-38.";
RL   Genome Announc. 1:E0013913-E0013913(2013).
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:EME59469.1}.
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DR   EMBL; AOEX01000063; EME59469.1; -; Genomic_DNA.
DR   RefSeq; WP_003938076.1; NZ_AOEX01000063.1.
DR   AlphaFoldDB; M2ZGL1; -.
DR   PATRIC; fig|1278076.4.peg.4129; -.
DR   Proteomes; UP000011731; 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"
FT   COMPBIAS        22..36
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  14707 MW;  2BF3BC5BF02DC302 CRC64;
     MSQTENQKAK RIPLGKDAST RRRLSKQRRH FRLRKKVAGT AERPRLVVNR SSRHLHAQLV
     DDLTGTTLAA ASTVEPDVRA LQGDKKARGA KVGQLIAERA KAAGVEAVVF DRGGHTYSGR
     IAALADAARE SGLKF
//
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