ID A0A286GF33_9ACTN Unreviewed; 282 AA.
AC A0A286GF33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN06272739_0590 {ECO:0000313|EMBL:SOD94112.1};
OS Blastococcus haudaquaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOD94112.1, ECO:0000313|Proteomes:UP000219482};
RN [1] {ECO:0000313|Proteomes:UP000219482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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}.
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DR EMBL; OCNK01000001; SOD94112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GF33; -.
DR Proteomes; UP000219482; 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:UP000219482};
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 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 29473 MW; C185FF64E5943C22 CRC64;
MSQSIDTRTD RQVDVRTPAG ETSGSVTLPG ELFDASANVS LMHQVVVAQL AAARQGTHAT
KTRAMVSGGG VKPYRQKGTG RARQGSIRAP QFTGGGIVHG PQPRDYTKKT PKKMKAAALR
GALSDRAREG RVHVVSAFVD GDAPKTKAAL ATLNAVTQAK RVLIVLDRDD VLNWVSLRNV
PQVHLIEAGQ LNTYDVLVAD EVVFTETALA EFVAGPAKGK QLPDVSTTVV TGIPSVAPAE
GEGTVETTAS EAPAKKAAAK KAPAKKAAAE KPAADENSEE KA
//
