ID D0GL32_9FUSO Unreviewed; 214 AA.
AC D0GL32;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:EEY35159.1};
GN ORFNames=HMPREF0554_0284 {ECO:0000313|EMBL:EEY35159.1};
OS Pseudoleptotrichia goodfellowii F0264.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Pseudoleptotrichia.
OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35159.1, ECO:0000313|Proteomes:UP000004226};
RN [1] {ECO:0000313|EMBL:EEY35159.1, ECO:0000313|Proteomes:UP000004226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0264 {ECO:0000313|EMBL:EEY35159.1,
RC ECO:0000313|Proteomes:UP000004226};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (OCT-2009) 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:EEY35159.1}.
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DR EMBL; ADAD01000104; EEY35159.1; -; Genomic_DNA.
DR RefSeq; WP_006807204.1; NZ_ADAD01000104.1.
DR AlphaFoldDB; D0GL32; -.
DR eggNOG; COG0088; Bacteria.
DR Proteomes; UP000004226; 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:UP000004226};
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..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 214 AA; 23700 MW; 87AAB09B8AA304F6 CRC64;
MPVLNTYKLD GSKAGTVEVK EEIFGIEPNK TVMHEVLVAE LAGAREGNAS TKTRAEVRGG
GRKPFRQKGT GRARQGSTRA PHMVGGGVVH GPKPRDYTKK VNKKVRRLAL RSALATKINN
GDLIVLDDFT LDVPKTKTFV QFAKALNFAG EKQLFIADYN GETFNRDINL EYSVRNLEKV
MTLDSRSLSI FWLIKQDKIV VTKEALATIE EVLA
//
