ID A0A0F6TCR3_9CORY Unreviewed; 217 AA.
AC A0A0F6TCR3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ECO:0000313|EMBL:AKE40546.1};
GN ORFNames=UL82_01590 {ECO:0000313|EMBL:AKE40546.1};
OS Corynebacterium kutscheri.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE40546.1, ECO:0000313|Proteomes:UP000033457};
RN [1] {ECO:0000313|EMBL:AKE40546.1, ECO:0000313|Proteomes:UP000033457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE40546.1,
RC ECO:0000313|Proteomes:UP000033457};
RX PubMed=26021937;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT DNA.";
RL Genome Announc. 3:e00571-15(2015).
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. {ECO:0000256|HAMAP-
CC 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; CP011312; AKE40546.1; -; Genomic_DNA.
DR RefSeq; WP_046438639.1; NZ_LR134407.1.
DR AlphaFoldDB; A0A0F6TCR3; -.
DR STRING; 35755.UL82_01590; -.
DR KEGG; cku:UL82_01590; -.
DR HOGENOM; CLU_041575_5_0_11; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000033457; 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:UP000033457};
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 45..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 23746 MW; 8CECD7FEA6E6AD36 CRC64;
MTNLTLDVHT AEGKVDGSVE LPAEIFDREV SVALLHQVVN AQLAAKRQGT HSTKTRGEVR
GGGRKPFRQK GTGRARQGSI RAPHFTGGGI SHGPKPRDYS QRTPKKMIKA ALYGALSDRA
RHERIHVVSE LVAGQTPSTK SARAFIERLT DRRNVLFVVG REDITAQKSA RNLPGVQILF
SDQLNTYDVL KSDDVVFSVE ALHTFIARAT GAAKEEN
//
