ID RL4_WOLTR Reviewed; 204 AA.
AC Q5GSU5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000255|HAMAP-Rule:MF_01328};
DE AltName: Full=50S ribosomal protein L4 {ECO:0000305};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Wbm0340;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR EMBL; AE017321; AAW70929.1; -; Genomic_DNA.
DR RefSeq; WP_011256539.1; NC_006833.1.
DR AlphaFoldDB; Q5GSU5; -.
DR SMR; Q5GSU5; -.
DR STRING; 292805.Wbm0340; -.
DR KEGG; wbm:Wbm0340; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_1_5; -.
DR Proteomes; UP000000534; 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 Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_uL4_B; 1.
DR InterPro; IPR002136; Ribosomal_uL4.
DR InterPro; IPR013005; Ribosomal_uL4-like.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR NCBIfam; TIGR03953; rplD_bact; 1.
DR PANTHER; PTHR10746:SF6; 39S RIBOSOMAL PROTEIN L4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10746; 50S RIBOSOMAL PROTEIN L4; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..204
FT /note="Large ribosomal subunit protein uL4"
FT /id="PRO_0000242460"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 23075 MW; 007B2ED37C78739F CRC64;
MECKLVNLSN NDVGTTQLNP LIFSVEQKLS ILHDIVRWQL AKRRAGTHKV KGISDVSGTT
AKPYSQKRTG RARQGSLRSP QFRGGGVIFG PIVRSHAYSL NKKVRKFGLK VALSLKYLNN
QVIILNNLNI NVKKTSEMCK YIQNFKFSSF LIVGDYEDSL LRAARNLHYV NLIKPIGLNV
FDILNHECIM LTSDALRYLE GRLL
//
