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RL4_METHJ
ID   RL4_METHJ               Reviewed;         249 AA.
AC   Q2FU92;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Mhun_2252;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD41957.1; -; Genomic_DNA.
DR   RefSeq; WP_011449215.1; NC_007796.1.
DR   AlphaFoldDB; Q2FU92; -.
DR   SMR; Q2FU92; -.
DR   STRING; 323259.Mhun_2252; -.
DR   EnsemblBacteria; ABD41957; ABD41957; Mhun_2252.
DR   GeneID; 3924213; -.
DR   KEGG; mhu:Mhun_2252; -.
DR   eggNOG; arCOG04071; Archaea.
DR   HOGENOM; CLU_026535_0_0_2; -.
DR   OMA; WHQKVNV; -.
DR   OrthoDB; 65833at2157; -.
DR   Proteomes; UP000001941; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..249
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242469"
SQ   SEQUENCE   249 AA;  27238 MW;  018AB63B925A6277 CRC64;
     MKAQVLTLTG SVAHEIELPP VFSSEFRPDL IKKAVIAQQS RRYQPHGAYV YAGITASAVG
     WGSGRGVSHV PRLKNSSRAA KVPQAKGGRE AHPPKVEKVL IRNINQKEKR KALNSAIAAT
     ISPELVRSRG HVFTGSLPYV LSGDFESLKK TKEVIAALRA VGVYGDVERA ERSRKVRAGR
     GKLRGRRYKQ RKSLLIVTGK ERLRAARNLA GVDVCLVDNL NVELLAPGTH SARLTLWTED
     AVRKLGGEQ
 
 
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