ID F2IUU8_POLGS Unreviewed; 105 AA.
AC F2IUU8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=SL003B_1750 {ECO:0000313|EMBL:ADZ70177.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ70177.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ70177.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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}.
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DR EMBL; CP002568; ADZ70177.1; -; Genomic_DNA.
DR RefSeq; WP_013652494.1; NC_015259.1.
DR AlphaFoldDB; F2IUU8; -.
DR STRING; 991905.SL003B_1750; -.
DR KEGG; pgv:SL003B_1750; -.
DR PATRIC; fig|991905.3.peg.1794; -.
DR eggNOG; COG0198; Bacteria.
DR HOGENOM; CLU_093315_2_2_5; -.
DR OrthoDB; 9807419at2; -.
DR Proteomes; UP000008130; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000008130};
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 4..31
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
SQ SEQUENCE 105 AA; 11312 MW; 9DFB8F13973F1978 CRC64;
MAAKIKKGDT VVVLTGRDKG KTGEVIQMMP AENKALVRGV NVVRRHQRQT QTQEGGIVAK
EAPIHVSNIA VADPKDGKAT RVGFKVQEDG RKVRVAKRSG DLIDG
//
