RL4_METM5
ID RL4_METM5 Reviewed; 252 AA.
AC A4FVY1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MmarC5_0032;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-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; CP000609; ABO34349.1; -; Genomic_DNA.
DR RefSeq; WP_011867811.1; NC_009135.1.
DR AlphaFoldDB; A4FVY1; -.
DR SMR; A4FVY1; -.
DR STRING; 402880.MmarC5_0032; -.
DR EnsemblBacteria; ABO34349; ABO34349; MmarC5_0032.
DR GeneID; 4928222; -.
DR KEGG; mmq:MmarC5_0032; -.
DR eggNOG; arCOG04071; Archaea.
DR HOGENOM; CLU_026535_0_0_2; -.
DR OMA; WHQKVNV; -.
DR OrthoDB; 65833at2157; -.
DR Proteomes; UP000000253; 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..252
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000142150"
SQ SEQUENCE 252 AA; 26966 MW; 7711ED16C5991137 CRC64;
MNVKVYNLDG SEKGDIELPA VFETEYRPDL IKRAVISSLT AKLQPKGCDA FAGYRTSAKS
IGKGHGKARV RRTAQGAGAF VPQAVGGRRA HPPKVEKILF ERINKKEKLK ALASAIAASA
IPEIVSARGH KIEGVPSLPL VVNAEFEGLV KTKEVLDVFK ALNLAADVEK AKDGIKIKAG
RAKLRGRKYK KPRSVLVVVG DACEAIAASR NLAGVDVITA NDLSAIHIAP GTMAGRLTLW
TENAIEKING RF