RL4_METMA
ID RL4_METMA Reviewed; 253 AA.
AC Q8PV49;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MM_2125;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31821.1; -; Genomic_DNA.
DR RefSeq; WP_011034056.1; NC_003901.1.
DR AlphaFoldDB; Q8PV49; -.
DR SMR; Q8PV49; -.
DR STRING; 192952.MM_2125; -.
DR EnsemblBacteria; AAM31821; AAM31821; MM_2125.
DR GeneID; 24840301; -.
DR KEGG; mma:MM_2125; -.
DR PATRIC; fig|192952.21.peg.2439; -.
DR eggNOG; arCOG04071; Archaea.
DR HOGENOM; CLU_026535_0_0_2; -.
DR OMA; WHQKVNV; -.
DR Proteomes; UP000000595; 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..253
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129334"
FT REGION 62..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; 27481 MW; D302B3DCE7184FDC CRC64;
MATAKTIDLT GRTVGEIELP AVFDADYRPD LIKKAVLAAQ ANRLQPYGPS LYAGMKTSAT
GWGSGRGVSH VPRLKNSSRA ARVPHAKGGR RAHPPKPEAD RSEKVNTKER RYAIRSAIAA
TIDPTLVNLR GHIFEAELPI VAVNDLENLE RTKQVIEFLE AAGLYEDVLR AKYGRHIRAG
RGKLRGRKYK HKKSVLIVAG ENSPILKAAR NLSGVDVVTV DSLNAELLAP GTHAGRLTVW
TESAIGKLEG AFQ