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Database: UniProt
Entry: A0A3Q9G427_9GAMM
LinkDB: A0A3Q9G427_9GAMM
Original site: A0A3Q9G427_9GAMM 
ID   A0A3Q9G427_9GAMM        Unreviewed;       201 AA.
AC   A0A3Q9G427;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=EKO29_01375 {ECO:0000313|EMBL:AZQ82819.1};
OS   Colwellia sp. Arc7-635.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=2497879 {ECO:0000313|EMBL:AZQ82819.1, ECO:0000313|Proteomes:UP000286937};
RN   [1] {ECO:0000313|EMBL:AZQ82819.1, ECO:0000313|Proteomes:UP000286937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arc7-635 {ECO:0000313|EMBL:AZQ82819.1,
RC   ECO:0000313|Proteomes:UP000286937};
RA   Lin J.;
RT   "Complete Genome Sequences of Colwellia sp. Arc7-635, a Denitrifying
RT   Bacterium Isolated from Arctic Seawater.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP034660; AZQ82819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9G427; -.
DR   KEGG; cov:EKO29_01375; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000286937; 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   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          44..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  21878 MW;  83B4AA02063B4F66 CRC64;
     MELALKDASG ALEVSETTFG LEFNEALVHQ VVVAYAAGAR AGTRAQKTRS EVSGGGAKPW
     RQKGTGRARA GTSRGPIWRT GGVTFAAKPQ DHSQKVNRKM YRGAIKSILS ELVRQERLVV
     VENFAVETPK TKELVAKLNA LELKDVLIVT PEIDENLFLS ARNLYKVDVR DVDGIDPVSL
     VGFEKVLMTA SAVKQLEEML G
//
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