ID RL3_BURMS Reviewed; 219 AA. AC A1V8A3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000255|HAMAP-Rule:MF_01325}; DE AltName: Full=50S ribosomal protein L3 {ECO:0000305}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=BMASAVP1_A3169; OS Burkholderia mallei (strain SAVP1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320388; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAVP1; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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 L19. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family. CC {ECO:0000255|HAMAP-Rule:MF_01325}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000526; ABM51145.1; -; Genomic_DNA. DR RefSeq; WP_004521904.1; NC_008785.1. DR AlphaFoldDB; A1V8A3; -. DR SMR; A1V8A3; -. DR GeneID; 56594543; -. DR KEGG; bmv:BMASAVP1_A3169; -. DR HOGENOM; CLU_044142_4_1_4; -. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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; 3.30.160.810; -; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_01325_B; Ribosomal_uL3_B; 1. DR InterPro; IPR000597; Ribosomal_uL3. DR InterPro; IPR019927; Ribosomal_uL3_bac/org-type. DR InterPro; IPR019926; Ribosomal_uL3_CS. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR03625; L3_bact; 1. DR PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1. DR PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. PE 3: Inferred from homology; KW Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..219 FT /note="Large ribosomal subunit protein uL3" FT /id="PRO_1000052024" FT REGION 133..153 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..147 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 153 FT /note="N5-methylglutamine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325" SQ SEQUENCE 219 AA; 22967 MW; 01C1529B9090BA8F CRC64; MSLGLVGRKV GMTRIFTAEG DSIPVTVLDV SDNRVTQIKT VETDGYTAVQ VAFGSRRASR VTKPLAGHLA KAGVEAGEIL KEFRIEADKA AELSNGAVIG PDLFEVGQKV DVQGVSIGKG YAGTIKRYNF GSGRASHGNS RSHNVPGSIG MAQDPGRVFP GKRMTGHMGD ETVTVQNLEI ARIDADRKLL LVKGAVPGAK GGKVFVTPAV KTRAVKGAK //