ID V8G8F3_9BURK Unreviewed; 106 AA.
AC V8G8F3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:ETD72814.1};
GN ORFNames=V757_02070 {ECO:0000313|EMBL:ETD72814.1};
OS Pelistega indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pelistega.
OX NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72814.1, ECO:0000313|Proteomes:UP000018766};
RN [1] {ECO:0000313|EMBL:ETD72814.1, ECO:0000313|Proteomes:UP000018766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM-7 {ECO:0000313|EMBL:ETD72814.1,
RC ECO:0000313|Proteomes:UP000018766};
RA Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT "Genomic analysis of Pelistega sp. HM-7.";
RL Submitted (NOV-2013) 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:ETD72814.1}.
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DR EMBL; AYSV01000017; ETD72814.1; -; Genomic_DNA.
DR RefSeq; WP_023949376.1; NZ_CABMIG010000017.1.
DR AlphaFoldDB; V8G8F3; -.
DR PATRIC; fig|1414851.3.peg.432; -.
DR OrthoDB; 9807419at2; -.
DR Proteomes; UP000018766; 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; 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; PF17136; ribosomal_L24; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018766};
KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000313|EMBL:ETD72814.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
SQ SEQUENCE 106 AA; 11399 MW; 545B79CA7CD4BC87 CRC64;
MNKIRKGDEV IVIAGRDKKR RGVVLARVDA DHVLVEGVNV AKKHQKPNPM TGAQGGVVDK
TMPIHVSNVA IFNPATGKAD RVGIKEVDGH KVRVYRSNGE VVGVKA
//
