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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
 
 
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