ID   RL4_METM6               Reviewed;         252 AA.
AC   A9A9B7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MmarC6_1126;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX01940.1; -; Genomic_DNA.
DR   RefSeq; WP_012193883.1; NC_009975.1.
DR   AlphaFoldDB; A9A9B7; -.
DR   SMR; A9A9B7; -.
DR   STRING; 444158.MmarC6_1126; -.
DR   EnsemblBacteria; ABX01940; ABX01940; MmarC6_1126.
DR   GeneID; 5738786; -.
DR   KEGG; mmx:MmarC6_1126; -.
DR   eggNOG; arCOG04071; Archaea.
DR   HOGENOM; CLU_026535_0_0_2; -.
DR   OMA; WHQKVNV; -.
DR   OrthoDB; 65833at2157; -.
DR   PhylomeDB; A9A9B7; -.
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..252
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000142151"
SQ   SEQUENCE   252 AA;  26943 MW;  748737B68C89948E CRC64;
     MNVKVYNLDG SEKGDIELPA VFETEYRPDL IKRAVISSLT AKLQPKGCDA FAGYRTSAKS
     IGKGHGKARV RRTAQGAGAF VPQAVGGRRA HPPKVEKILF ERINRKERLK ALASAIAASA
     NPEIVSARGH KIEGVPSLPL VVNAEFESLA KTKEVLGVFT ALKLDADLER AKDGVKIKAG
     RAKLRGRKYK KPKSVLVVVG DACDAVAASR NLAGVDVITA NDLSAIHIAP GTMAGRLTLW
     TESAIEKLNG RF