RL4_METS3
ID RL4_METS3 Reviewed; 254 AA.
AC A5UL88;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Msm_0761;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86966.1; -; Genomic_DNA.
DR RefSeq; WP_004033203.1; NC_009515.1.
DR AlphaFoldDB; A5UL88; -.
DR SMR; A5UL88; -.
DR STRING; 420247.Msm_0761; -.
DR EnsemblBacteria; ABQ86966; ABQ86966; Msm_0761.
DR GeneID; 5215996; -.
DR KEGG; msi:Msm_0761; -.
DR PATRIC; fig|420247.28.peg.758; -.
DR eggNOG; arCOG04071; Archaea.
DR HOGENOM; CLU_026535_0_0_2; -.
DR OMA; WHQKVNV; -.
DR Proteomes; UP000001992; Chromosome.
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_A; Ribosomal_L4_A; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR InterPro; IPR019970; Ribosomall_L4-archaea.
DR PANTHER; PTHR19431; PTHR19431; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03672; rpl4p_arch; 1.
DR PROSITE; PS00939; RIBOSOMAL_L1E; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..254
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000142155"
FT REGION 45..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 27972 MW; 34D560DFAC605FB1 CRC64;
MKANVYSMEG EVKEEIELPA IFNEEYRPDL IKRAVISAQT ARVQPWGNDP EAGKRTSAKG
WGSGRGTARV PRIKNGSKAA FVPMAVGGRR AHPTRAEKNH HEKINIKERR FAIRSAVAAT
ANKELVENRG HRLGDLEQVP IIVEDDICSV KTTKQTREIF QNLGVYDDIT RAKEGKRIRA
GRGKTRGRKY KKVKGPLLVV GEDNGIKLGA RNHAGVDVVT VENLNAELLA PGTHPGRLTI
FTKSAVEKLG GLFQ