RL4_METVS
ID RL4_METVS Reviewed; 252 AA.
AC A6UQJ1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Mevan_0858;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR54763.1; -; Genomic_DNA.
DR RefSeq; WP_011972664.1; NC_009634.1.
DR AlphaFoldDB; A6UQJ1; -.
DR SMR; A6UQJ1; -.
DR STRING; 406327.Mevan_0858; -.
DR EnsemblBacteria; ABR54763; ABR54763; Mevan_0858.
DR GeneID; 5324918; -.
DR KEGG; mvn:Mevan_0858; -.
DR eggNOG; arCOG04071; Archaea.
DR HOGENOM; CLU_026535_0_0_2; -.
DR OMA; WHQKVNV; -.
DR OrthoDB; 65833at2157; -.
DR Proteomes; UP000001107; 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_1000142157"
SQ SEQUENCE 252 AA; 27134 MW; 0434D38E484BFCFD CRC64;
MNVKVYNLDG SEKGAIELPS VFETEYRPDV IKRAVISSLT ARLQPKGSDP LAGYRTSAKS
IGKGHGKARV RRTAQGAGAF VPQAVGGRRA HPPKVEKILF ERINRKERLK ALASAIAASA
NSEIVAARGH KIEGVPSLPL VVNAEFESLV KTKEVLSVFK ALKLEADLER AKDGIKIKAG
RAKLRGRKYK KPRSVLVVVG DACDAVAASR NLAGVDVITA NDLSAIHIAP GTMAGRLTLW
TENAIEKLKE RF