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Database: UniProt
Entry: A0A2Z2NKB8_9GAMM
LinkDB: A0A2Z2NKB8_9GAMM
Original site: A0A2Z2NKB8_9GAMM 
ID   A0A2Z2NKB8_9GAMM        Unreviewed;       200 AA.
AC   A0A2Z2NKB8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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:ASJ71842.1};
GN   ORFNames=IMCC3135_08720 {ECO:0000313|EMBL:ASJ71842.1};
OS   Granulosicoccus antarcticus IMCC3135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Granulosicoccaceae; Granulosicoccus.
OX   NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ71842.1, ECO:0000313|Proteomes:UP000250079};
RN   [1] {ECO:0000313|EMBL:ASJ71842.1, ECO:0000313|Proteomes:UP000250079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ71842.1,
RC   ECO:0000313|Proteomes:UP000250079};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; CP018632; ASJ71842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2NKB8; -.
DR   KEGG; gai:IMCC3135_08720; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000250079; Chromosome.
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:UP000250079};
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          45..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  21460 MW;  22631600DBADA102 CRC64;
     MDLKTHSGGS VSVADSVFGV DYNEGLVHQI VTAYLAAARA GTSAQKTRSE VSGGGAKPWR
     QKGTGRARAG TSRSPIWTGG GVTFASKTRD YSQKVNKKMY RGAIRSILSH AAAEGRLIVV
     DSLEVTESKT KAMKAKMAEL GVKKVLFLMD DVTESVYLAS RNIPYVQVLD VEGVDPVSLV
     RFPHIVATAA AVKQLEERFS
//
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