ID A0A2A9F8H4_9PSEU Unreviewed; 229 AA.
AC A0A2A9F8H4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=ATK36_2691 {ECO:0000313|EMBL:PFG47644.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG47644.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG47644.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG47644.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG47644.1}.
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DR EMBL; PDJK01000002; PFG47644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9F8H4; -.
DR Proteomes; UP000243542; 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:UP000243542};
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 43..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 24426 MW; 84F037E8248BECCC CRC64;
MTSVELKTPA GKADGTLELP AEIFDVQANI ALMHQVVVAQ QAAARQGTHD TKTRGEVSGG
GKKPYRQKGT GRARQGSTRA PQFTGGGVVH GPTPRDYSQR TPKKMKAAAL RGALSDRARA
GQLHVVTELV TGEKPSTKAA KTALAGVTQA KRVLVVLHRG EELSWVSLRN LPEIHLIWAD
QLNTYDVLVN DDVVFTRAAY EAFVAGPVRG KGAKAVARES EVAEGSDDK
//