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Database: UniProt
Entry: A0A1R4GRW4_9GAMM
LinkDB: A0A1R4GRW4_9GAMM
Original site: A0A1R4GRW4_9GAMM 
ID   A0A1R4GRW4_9GAMM        Unreviewed;       200 AA.
AC   A0A1R4GRW4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:SJM70929.1};
GN   ORFNames=A1232T_01100 {ECO:0000313|EMBL:SJM70929.1};
OS   Psychrobacter piechaudii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1945521 {ECO:0000313|EMBL:SJM70929.1, ECO:0000313|Proteomes:UP000188357};
RN   [1] {ECO:0000313|EMBL:SJM70929.1, ECO:0000313|Proteomes:UP000188357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Psychrobacter_piechaudii {ECO:0000313|EMBL:SJM70929.1};
RA   Peterson S.W.;
RL   Submitted (FEB-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; FUGE01000119; SJM70929.1; -; Genomic_DNA.
DR   RefSeq; WP_028858248.1; NZ_FUGE01000119.1.
DR   AlphaFoldDB; A0A1R4GRW4; -.
DR   STRING; 1945521.A1232T_01100; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000188357; 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:UP000188357};
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          44..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  21927 MW;  EC47466F00A0BBFC CRC64;
     MNLKTVTGAA VELSDTAFGR EFNEALVHQV VTAYLAGARQ GTRAQKTRAE VSGGGKKPWR
     QKGTGRARAG SIRSPIWRSG GRAFAAKPQD WSQKVNRKMY RGAMQCILAE LVRQDRLILV
     EDITVSAPKT KELISKLEEL NAPRALIVTN EVDENLYLAA RNIPHVNVLG TNEVDPVSLI
     AFDKVIMSVD AAKQFEEALA
//
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