ID A0A2A5W2C0_9BACT Unreviewed; 80 AA.
AC A0A2A5W2C0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 ECO:0000313|EMBL:PDH30521.1};
GN ORFNames=CNC89_00120 {ECO:0000313|EMBL:PDH30521.1};
OS Puniceicoccaceae bacterium MED-G31.
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales; Puniceicoccaceae.
OX NCBI_TaxID=1986245 {ECO:0000313|EMBL:PDH30521.1, ECO:0000313|Proteomes:UP000219700};
RN [1] {ECO:0000313|EMBL:PDH30521.1, ECO:0000313|Proteomes:UP000219700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G31 {ECO:0000313|EMBL:PDH30521.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:PDH30521.1}.
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DR EMBL; NTJW01000001; PDH30521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5W2C0; -.
DR Proteomes; UP000219700; 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; IPR041988; Ribosomal_uL24_KOW.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR NCBIfam; TIGR01079; rplX_bact; 1.
DR PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000313|EMBL:PDH30521.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT DOMAIN 10..36
FT /note="KOW"
FT /evidence="ECO:0000259|Pfam:PF00467"
SQ SEQUENCE 80 AA; 8888 MW; 9A56BFD29E81037F CRC64;
MAKVIKREQE VVVISGAHRG KRGKVLEVKA GEKILVEGVN LVTKYERKTQ DNPDGGSVEK
EAPLHYSNVV LAEKYDAKKK
//
