ID D5X9W2_THEPJ Unreviewed; 206 AA.
AC D5X9W2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|ARBA:ARBA00035244, ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328};
GN OrderedLocusNames=TherJR_0297 {ECO:0000313|EMBL:ADG81183.1};
OS Thermincola potens (strain JR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC Thermincola.
OX NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG81183.1, ECO:0000313|Proteomes:UP000002377};
RN [1] {ECO:0000313|EMBL:ADG81183.1, ECO:0000313|Proteomes:UP000002377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR {ECO:0000313|EMBL:ADG81183.1,
RC ECO:0000313|Proteomes:UP000002377};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000256|HAMAP-Rule:MF_01328}.
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:0000256|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00011838, ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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DR EMBL; CP002028; ADG81183.1; -; Genomic_DNA.
DR RefSeq; WP_013119208.1; NC_014152.1.
DR AlphaFoldDB; D5X9W2; -.
DR STRING; 635013.TherJR_0297; -.
DR KEGG; tjr:TherJR_0297; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_9; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000002377; 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_L4_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 {ECO:0000313|Proteomes:UP000002377};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01328};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT REGION 48..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 206 AA; 22445 MW; D84D74E1B8C52E4D CRC64;
MPKVALYNIK GEQVGEIELK DEVFGIEPNE GLVHDVVVMQ LANRRVGTAS TKTRAEVSGG
GRKPWRQKGT GRARHGSIRS PIWRGGGITF GPKPRSFNYT MPKKARRLAL KSVLSSKVSD
GNIIVLDTLE MAQPKTKEMA EILNRLKAKK AVVVTADVDQ NVIKSARNIP GVTPLTASGL
NVYDLVNHEK LVITKDAVAK VEEVLA
//
