ID   RL4_METBF               Reviewed;         253 AA.
AC   Q46G96;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Mbar_A0109;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69096.1; -; Genomic_DNA.
DR   RefSeq; WP_011305151.1; NC_007355.1.
DR   AlphaFoldDB; Q46G96; -.
DR   SMR; Q46G96; -.
DR   STRING; 269797.Mbar_A0109; -.
DR   EnsemblBacteria; AAZ69096; AAZ69096; Mbar_A0109.
DR   GeneID; 3626231; -.
DR   KEGG; mba:Mbar_A0109; -.
DR   eggNOG; arCOG04071; Archaea.
DR   HOGENOM; CLU_026535_0_0_2; -.
DR   OMA; WHQKVNV; -.
DR   OrthoDB; 65833at2157; -.
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; 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.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..253
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242467"
FT   REGION          61..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  27767 MW;  5202F55C9B2E8E3A CRC64;
     MATAKTIDLT GKVVREIELP DVFDVDYRPD LIKKAVLAAQ ANRLQPYGPR LYAGMETSAR
     GWGSGRGTSH VPRLVNSSRA ARVPHARGGR RAHPPKPEAD RSEKVNTKER RYAIRSAIAA
     TRDPTLVSLR GHIFEAELPI VTENALEDLD KTKQVIEFLQ AIGVYEDVLR AKYGRHIRAG
     RGKLRGRKYK HKKSVLIVAG ESAPILKAAR NLSGVDVATV DSLNAELLAP GTHAGRLTIW
     TESAVEKLEG AFQ