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Database: UniProt
Entry: A0A1K1N494_RUMFL
LinkDB: A0A1K1N494_RUMFL
Original site: A0A1K1N494_RUMFL 
ID   A0A1K1N494_RUMFL        Unreviewed;       207 AA.
AC   A0A1K1N494;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN02910280_1687 {ECO:0000313|EMBL:SFW30069.1};
OS   Ruminococcus flavefaciens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265 {ECO:0000313|EMBL:SFW30069.1, ECO:0000313|Proteomes:UP000183461};
RN   [1] {ECO:0000313|EMBL:SFW30069.1, ECO:0000313|Proteomes:UP000183461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL228 {ECO:0000313|EMBL:SFW30069.1,
RC   ECO:0000313|Proteomes:UP000183461};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPIP01000003; SFW30069.1; -; Genomic_DNA.
DR   RefSeq; WP_028514309.1; NZ_FPIP01000003.1.
DR   AlphaFoldDB; A0A1K1N494; -.
DR   Proteomes; UP000183461; 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   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..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   207 AA;  22481 MW;  160AD286E49B3711 CRC64;
     MSTISVFDMT GKQVSETELN DEIFGITPNE GVMHAAVVNY LANQRQGTQS TLTRTEVSGG
     GRKPWRQKGT GHARQGSIRA PQWVHGGIAL GPKPRDYSYS LNKKVKRLAM KSALSTKVID
     NNMIVLDALT LEDYKTKTVV DMLKALGVEG KALIVTAEAD SKVIKSAANI PGVKTAAVNT
     LNVYDILNYD KFIVVKNAVG KIEEVYA
//
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