ID   RL3_METBU               Reviewed;         337 AA.
AC   Q12ZV1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Mbur_0001;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L24e. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; CP000300; ABE51025.1; -; Genomic_DNA.
DR   RefSeq; WP_011498189.1; NC_007955.1.
DR   AlphaFoldDB; Q12ZV1; -.
DR   SMR; Q12ZV1; -.
DR   STRING; 259564.Mbur_0001; -.
DR   EnsemblBacteria; ABE51025; ABE51025; Mbur_0001.
DR   GeneID; 3996831; -.
DR   KEGG; mbu:Mbur_0001; -.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   OrthoDB; 31722at2157; -.
DR   Proteomes; UP000001979; 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; 4.10.960.10; -; 1.
DR   HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR   InterPro; IPR045077; L3_arc_euk.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019928; Ribosomal_L3_arc.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11363; PTHR11363; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03626; L3_arch; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..337
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000052078"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  37077 MW;  330BF81292BF6177 CRC64;
     MAKGHRPRRG SLAYSPRKRS QSHIPRFRSW PESDAEPKLQ GFAGYKVGMT HVIMIDDVKH
     SLTEGTEISV PVTIIETPAI RVAAIRAYGK DTYGEIAIAE AWTDVLDKDL SRRLKTAKNP
     DVNASLEKLE TLVESGRAND IRLITYTLPS TLTGVPKKVP DVMETGVSGS DVKAKFEYAK
     TVLGTMVEIS DVFDNGKIVD VAAITTGHGT QGPVKRWGIN LMKNKHSRQG SLRQVGTLGP
     WTPAHVSWRV PQAGQMGYHQ RTDYNKRILK MSSDVDEVNP AGGFVNYGLV RGNYILIKGS
     VPGPSKRLIR LREPTRSKVS SIGEPQIMHV STQTLQG