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Database: UniProt
Entry: A0A316TN05_9BACT
LinkDB: A0A316TN05_9BACT
Original site: A0A316TN05_9BACT 
ID   A0A316TN05_9BACT        Unreviewed;       216 AA.
AC   A0A316TN05;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=DDZ15_16390 {ECO:0000313|EMBL:PWN05041.1};
OS   Rhodohalobacter mucosus.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC   Rhodohalobacter.
OX   NCBI_TaxID=2079485 {ECO:0000313|EMBL:PWN05041.1, ECO:0000313|Proteomes:UP000245533};
RN   [1] {ECO:0000313|EMBL:PWN05041.1, ECO:0000313|Proteomes:UP000245533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8A47 {ECO:0000313|EMBL:PWN05041.1,
RC   ECO:0000313|Proteomes:UP000245533};
RA   Liu Z.-W.;
RT   "Rhodohalobacter halophilus gen. nov., sp. nov., a moderately halophilic
RT   member of the family Balneolaceae.";
RL   Submitted (MAY-2018) 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. {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWN05041.1}.
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DR   EMBL; QGGB01000013; PWN05041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316TN05; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000245533; Unassembled WGS sequence.
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:UP000245533};
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..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   216 AA;  24053 MW;  1E316C67F5954E18 CRC64;
     MELTIYKVDG KSSGKKATLS DEIFAVEPNE TVLYEDVRRI LANRRQGTAK TKERSEVRGG
     GRKAYKQKGT GMARRGSMRS PLLKGGGTVF GPRPRTYTNN LNKKAKRLAR KSALSLKVSE
     DALKVVDDFT FEEIKTRQVV DMLTAFELEN SKVLIVTADT DHKLYLSARN IPGINVIEAF
     SPNTYDIMNS DIVLIQKSAI QVLENSIEPK VEEEAA
//
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