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Database: UniProt
Entry: A0A291GFE1_9RHOB
LinkDB: A0A291GFE1_9RHOB
Original site: A0A291GFE1_9RHOB 
ID   A0A291GFE1_9RHOB        Unreviewed;       206 AA.
AC   A0A291GFE1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CEW89_15075 {ECO:0000313|EMBL:ATG48770.1};
OS   Celeribacter ethanolicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG48770.1, ECO:0000313|Proteomes:UP000217935};
RN   [1] {ECO:0000313|EMBL:ATG48770.1, ECO:0000313|Proteomes:UP000217935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPH2 {ECO:0000313|EMBL:ATG48770.1,
RC   ECO:0000313|Proteomes:UP000217935};
RA   Woo J.-H., Kim H.-S.;
RT   "Celeribacter sp. TSPH2 complete genome sequence.";
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; CP022196; ATG48770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GFE1; -.
DR   STRING; 1758178.GCA_001550095_01445; -.
DR   KEGG; ceh:CEW89_15075; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000217935; 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:UP000217935};
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          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  22372 MW;  B6EA0537F1AABD3A CRC64;
     MKHDVIKLDG AKAGTLDLDE ALFGLEPRAD ILHRVVRWQR NNAQQGTHKV KTKSEVSYST
     KKIYRQKGTG GARHGSRKAP IFRKGGIYKG PTPRSHGHEL TKKFRKLGLK HALSAKAATG
     NLVVLDEAKL AEAKTALLAK AVKEQGWKRV LIIDGADIDA NFKAAAANIA GVDVLPTIGA
     NVYDILKRDT LVITKAGVEA LEARLK
//
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