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Database: UniProt
Entry: A0A0K8J2K7_9FIRM
LinkDB: A0A0K8J2K7_9FIRM
Original site: A0A0K8J2K7_9FIRM 
ID   A0A0K8J2K7_9FIRM        Unreviewed;       206 AA.
AC   A0A0K8J2K7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-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:CUH91871.1};
GN   ORFNames=SD1D_0318 {ECO:0000313|EMBL:CUH91871.1};
OS   Herbinix luporum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Herbinix.
OX   NCBI_TaxID=1679721 {ECO:0000313|EMBL:CUH91871.1, ECO:0000313|Proteomes:UP000196053};
RN   [1] {ECO:0000313|Proteomes:UP000196053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD1D {ECO:0000313|Proteomes:UP000196053};
RA   Wibberg D.;
RL   Submitted (SEP-2015) 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; LN879430; CUH91871.1; -; Genomic_DNA.
DR   RefSeq; WP_058257295.1; NZ_LN879430.1.
DR   AlphaFoldDB; A0A0K8J2K7; -.
DR   KEGG; hsd:SD1D_0318; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000196053; Chromosome i.
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:UP000196053};
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..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  22958 MW;  8B6C0ACA01989781 CRC64;
     MANVKVYNIE GKEVGTLELN DKVFGVEINE HLVHMAVVSQ LANKRQGTQS AKTRAEVRGG
     GRKPWRQKGT GHARQGSIRA PQWKGGGVVF APKPRDYSIK MNRKEKALAI KSALTSRVNA
     DKFLVLDQFG FDEIKTKKMK EVLNNLKVNK ALIVLDKKDA NVELSARNLP NVRTVLSNSI
     SVYDILKYDN LVITKDAVAQ IEEVYA
//
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