RL4_MYCPU
ID RL4_MYCPU Reviewed; 292 AA.
AC Q98PY2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MYPU_5870;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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: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}.
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DR EMBL; AL445565; CAC13760.1; -; Genomic_DNA.
DR PIR; C90585; C90585.
DR RefSeq; WP_010925388.1; NC_002771.1.
DR AlphaFoldDB; Q98PY2; -.
DR SMR; Q98PY2; -.
DR STRING; 272635.MYPU_5870; -.
DR EnsemblBacteria; CAC13760; CAC13760; CAC13760.
DR KEGG; mpu:MYPU_5870; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_2_0_14; -.
DR OMA; GTHDVKS; -.
DR OrthoDB; 1572673at2; -.
DR BioCyc; MPUL272635:G1GT6-599-MON; -.
DR Proteomes; UP000000528; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
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;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..292
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129245"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 32471 MW; 49C566E879801CE1 CRC64;
MVEVKKTTKT KSTEEKAPKI TKATKEKTSD KTALKAKTPK TKVSDKAEST PKKASVKTSA
KAEKINVEKT EKVEKVNVEK VSIKRESSSK DVQKADFSNI KELNSKIFEF EKNYDQAIFD
CILSERASRR QGTHKVKNRA EVSGTGKKPW KQKGTGKARA GSLRNPIFVG GGRAFGPSVN
RNYKISINKK VRLNALMASL FALAKSNSVL LKTFSLEKPS TKDLVEELRK INASNLKRIL
LVSDDKNIFL SARNLKNVKV TKVTSLMIED LVAADLLILS NENIKYLEGL IK
