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Database: UniProt
Entry: I9DQE7_9ALTE
LinkDB: I9DQE7_9ALTE
Original site: I9DQE7_9ALTE 
ID   I9DQE7_9ALTE            Unreviewed;       201 AA.
AC   I9DQE7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:EIW88240.1};
GN   ORFNames=AGRI_12077 {ECO:0000313|EMBL:EIW88240.1};
OS   Alishewanella agri BL06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW88240.1, ECO:0000313|Proteomes:UP000035062};
RN   [1] {ECO:0000313|EMBL:EIW88240.1, ECO:0000313|Proteomes:UP000035062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL06 {ECO:0000313|EMBL:EIW88240.1,
RC   ECO:0000313|Proteomes:UP000035062};
RX   PubMed=22933763; DOI=10.1128/JB.01129-12;
RA   Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT   Landfill Soil.";
RL   J. Bacteriol. 194:5135-5136(2012).
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:EIW88240.1}.
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DR   EMBL; AKKU01000023; EIW88240.1; -; Genomic_DNA.
DR   RefSeq; WP_008985230.1; NZ_AKKU01000023.1.
DR   AlphaFoldDB; I9DQE7; -.
DR   STRING; 1195246.AGRI_12077; -.
DR   PATRIC; fig|1195246.3.peg.2398; -.
DR   eggNOG; COG0088; Bacteria.
DR   Proteomes; UP000035062; 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:UP000035062};
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}.
SQ   SEQUENCE   201 AA;  22210 MW;  5AABA9E98BED33B8 CRC64;
     MELALRDAQG VLEVSEATFG REFNEALVHQ VVVAYAAGAR QGTRAQLTRS EVRGGGKKPW
     RQKGTGRARA GTIRSPIWRS GGVTFAAKPQ DHSQKVNRKM YRGAIQSILS ELVRQERLIV
     VENFGVESPK TKDLTAKLKA MDLKDVLIVT NEVDENLFLS ARNLYKVDVR DVHGIDPVSL
     IAFDKVLMTA AAVKQLEELL A
//
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