ID C9LGV0_9BACT Unreviewed; 209 AA.
AC C9LGV0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:EEX71908.1};
GN ORFNames=GCWU000325_01446 {ECO:0000313|EMBL:EEX71908.1};
OS Alloprevotella tannerae ATCC 51259.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX71908.1, ECO:0000313|Proteomes:UP000003460};
RN [1] {ECO:0000313|EMBL:EEX71908.1, ECO:0000313|Proteomes:UP000003460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX71908.1,
RC ECO:0000313|Proteomes:UP000003460};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-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:EEX71908.1}.
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DR EMBL; ACIJ02000018; EEX71908.1; -; Genomic_DNA.
DR RefSeq; WP_006255217.1; NZ_GG700642.1.
DR AlphaFoldDB; C9LGV0; -.
DR STRING; 626522.GCWU000325_01446; -.
DR GeneID; 84576372; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_10; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000003460; 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:UP000003460};
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 46..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 22958 MW; 9F6831DC605C1977 CRC64;
MEISVFNIKG EDTGRKAVLN EAVFGIEPND HAIYLDVKQY LAAQRQGTAK SKERSEMSGS
TRKLGRQKGG GGARRGDINS PVLVGGARVF GPRPRNYAFK LNKKLKALAR RSALSYKAKE
NSIVVLEDFT METPKTKAFV EILNNLKVSE KKVLVILPEA NKNVFLSARN LEGAKLAIAK
DINTYNVLDA GALVITERSL EDIDAVLNR
//