ID A0A090PA21_9VIBR Unreviewed; 200 AA.
AC A0A090PA21;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=EGH82_01275 {ECO:0000313|EMBL:ROV62338.1};
OS Vibrio ponticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=265668 {ECO:0000313|EMBL:ROV62338.1, ECO:0000313|Proteomes:UP000278792};
RN [1] {ECO:0000313|EMBL:ROV62338.1, ECO:0000313|Proteomes:UP000278792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1751 {ECO:0000313|EMBL:ROV62338.1,
RC ECO:0000313|Proteomes:UP000278792};
RA Soto-Rodriguez S., Lozano-Olvera R., Gomez-Gil B.;
RT "Vibrio ponticus strain CAIM 1751 pathogenic for the snapper Lutjanus
RT guttatus.";
RL Submitted (NOV-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}.
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:ROV62338.1}.
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DR EMBL; RKIK01000002; ROV62338.1; -; Genomic_DNA.
DR RefSeq; WP_075651050.1; NZ_RKIK01000002.1.
DR STRING; 265668.JCM19238_3383; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000278792; 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}.
SQ SEQUENCE 200 AA; 21855 MW; ACF5CE82E1A8C15F CRC64;
MELMVKGADA LTVSETTFGR EFNEALVHQV VVAFAAGARQ GTRAQKTRSE VSGGGAKPWR
QKGTGRARAG TIRSPIWRTG GVTFAAKPQD HSQKVNKKMY RGAMKSILSE LVRQERLIVV
DNFSVEAPKT KELVAKLKEL ELNDVLIVTG EVDENLFLAA RNLYKVDARD AAGIDPVSLI
AFDKVLMTAD AVKQVEEMLA
//
