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Database: UniProt
Entry: A0A0G0CX11_9BACT
LinkDB: A0A0G0CX11_9BACT
Original site: A0A0G0CX11_9BACT 
ID   A0A0G0CX11_9BACT        Unreviewed;       101 AA.
AC   A0A0G0CX11;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Large ribosomal subunit protein uL24 {ECO:0000256|ARBA:ARBA00035206, ECO:0000256|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000256|HAMAP-Rule:MF_01326};
GN   ORFNames=UR88_C0013G0011 {ECO:0000313|EMBL:KKP85603.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWA1_35_8.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618727 {ECO:0000313|EMBL:KKP85603.1, ECO:0000313|Proteomes:UP000186383};
RN   [1] {ECO:0000313|EMBL:KKP85603.1, ECO:0000313|Proteomes:UP000186383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000256|ARBA:ARBA00010618, ECO:0000256|HAMAP-Rule:MF_01326,
CC       ECO:0000256|RuleBase:RU003477}.
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:KKP85603.1}.
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DR   EMBL; LBQW01000013; KKP85603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0CX11; -.
DR   PATRIC; fig|1618727.3.peg.252; -.
DR   Proteomes; UP000186383; Unassembled WGS sequence.
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; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR003256; Ribosomal_uL24.
DR   InterPro; IPR005825; Ribosomal_uL24_CS.
DR   InterPro; IPR041988; Ribosomal_uL24_KOW.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   NCBIfam; TIGR01079; rplX_bact; 1.
DR   PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326,
KW   ECO:0000256|RuleBase:RU003477};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW   ECO:0000256|RuleBase:RU003477};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT   DOMAIN          2..29
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
SQ   SEQUENCE   101 AA;  11186 MW;  B369FD7FE3C8DB2E CRC64;
     MKLKKGDNVI IIAGKDKGKK GKIVAVFADK NRVVVEGINM MKKHQRPKKS GEKGTKINIA
     MPMNASNVMI VDPKTGLRTR IGKKRVGDKM VRITKKSSQE I
//
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