(data stored in ACNUC7421 zone)

SWISSPROT: RL4_PSEHT

ID   RL4_PSEHT               Reviewed;         201 AA.
AC   Q3IF24;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN   OrderedLocusNames=PSHAa0145;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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
CC       during the early stages of 50S assembly. It makes multiple
CC       contacts with different domains of the 23S rRNA in the assembled
CC       50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
DR   EMBL; CR954246; CAI85249.1; -; Genomic_DNA.
DR   RefSeq; WP_002957897.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF24; -.
DR   STRING; 326442.PSHAa0145; -.
DR   PRIDE; Q3IF24; -.
DR   EnsemblBacteria; CAI85249; CAI85249; PSHAa0145.
DR   GeneID; 32568430; -.
DR   KEGG; pha:PSHAa0145; -.
DR   eggNOG; ENOG4106U5A; Bacteria.
DR   eggNOG; COG0088; LUCA.
DR   HOGENOM; HOG000248766; -.
DR   KO; K02926; -.
DR   OMA; DYSFKLN; -.
DR   OrthoDB; POG091H027V; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.40.1370.10; -; 2.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03953; rplD_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IF24.
DR   SWISS-2DPAGE; Q3IF24.
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1    201       50S ribosomal protein L4.
FT                                /FTId=PRO_0000242415.
SQ   SEQUENCE   201 AA;  21829 MW;  4E041D8AB510B4AA CRC64;
     MELAIKDASG GLEVSEATFG REFNEALVHQ VVVAYAAGAR QGTRAQKTRS EVSGGGKKPW
     AQKGTGRARA GTIRSPIWRS GGVSFAAKPQ DHSQKVNRKM YRGAIKSILS ELVRQERLIV
     VESFALAAPK TKELVAKLKE LELKDVLIVT EEVDENLFLS ARNLYKVDTR DVAGIDPVSL
     IAFDKVLITA AAVKQLEEAL A
//

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