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Database: UniProt
Entry: A0A370DKZ7_9GAMM
LinkDB: A0A370DKZ7_9GAMM
Original site: A0A370DKZ7_9GAMM 
ID   A0A370DKZ7_9GAMM        Unreviewed;       204 AA.
AC   A0A370DKZ7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=DIZ78_11550 {ECO:0000313|EMBL:RDH85585.1};
OS   endosymbiont of Escarpia spicata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2200908 {ECO:0000313|EMBL:RDH85585.1, ECO:0000313|Proteomes:UP000254771};
RN   [1] {ECO:0000313|EMBL:RDH85585.1, ECO:0000313|Proteomes:UP000254771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1462 {ECO:0000313|EMBL:RDH85585.1};
RX   PubMed=30022157;
RA   Li Y., Liles M.R., Halanych K.M.;
RT   "Endosymbiont genomes yield clues of tubeworm success.";
RL   ISME J. 0:0-0(2018).
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:RDH85585.1}.
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DR   EMBL; QFXE01000013; RDH85585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370DKZ7; -.
DR   Proteomes; UP000254771; 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:UP000254771};
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          47..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22168 MW;  F3C9A88C3F63C983 CRC64;
     MDLNVTSAGG DAQTIQVSDD VFGAAYNEGL VHQVVTAHMA AARAGTKAQK NRAAVRGGGA
     KPWRQKGTGR ARSGTIRSPI WRSGGVTFAA SPRNFAQKVN RKMYRGAIRS ILSELVRQER
     FVAVNEFAVS APKTKELAGK LKEMNLKDVL VVAENPDENL YLAARNLYGV DVRDVNEIDP
     VSLVAYEKVL MTEGAVKKIE ERLA
//
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