ID I3YWM4_AEQSU Unreviewed; 104 AA.
AC I3YWM4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Aeqsu_1918 {ECO:0000313|EMBL:AFL81392.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81392.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL81392.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003280; AFL81392.1; -; Genomic_DNA.
DR RefSeq; WP_014782646.1; NC_018013.1.
DR AlphaFoldDB; I3YWM4; -.
DR STRING; 746697.Aeqsu_1918; -.
DR KEGG; asl:Aeqsu_1918; -.
DR PATRIC; fig|746697.3.peg.1952; -.
DR eggNOG; COG0198; Bacteria.
DR HOGENOM; CLU_093315_2_0_10; -.
DR OrthoDB; 9807419at2; -.
DR Proteomes; UP000006049; 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; 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.
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:AFL81392.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT DOMAIN 5..32
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
SQ SEQUENCE 104 AA; 11151 MW; 4CF288AEC9B86AFC CRC64;
MTKLKIKSGD TVVVTAGDHK GSEGKVMKIL LDKNKAIVEG VNMVSKHEKP SAKNPQGGIA
KKEAPIHISN LSLVDPKSGK ATRVGYKTEN GKKVRFSKQS NQAI
//
