ID K4L2Z1_9FIRM Unreviewed; 209 AA.
AC K4L2Z1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325,
GN ECO:0000313|EMBL:AFV05900.1};
GN ORFNames=DCF50_p1898 {ECO:0000313|EMBL:AFV05900.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV05900.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV05900.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV05900.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000256|ARBA:ARBA00006540, ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003905}.
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; CP003870; AFV05900.1; -; Genomic_DNA.
DR RefSeq; WP_015043942.1; NC_018867.1.
DR AlphaFoldDB; K4L2Z1; -.
DR STRING; 1131462.DCF50_p1898; -.
DR KEGG; dec:DCF50_p1898; -.
DR PATRIC; fig|1131462.4.peg.1915; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_9; -.
DR Proteomes; UP000000482; Chromosome.
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_L3_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 Reference proteome {ECO:0000313|Proteomes:UP000000482};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906}.
FT REGION 116..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..137
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 22774 MW; 0A4A22B1127AAC1C CRC64;
MSRGILGKKV GMTQIFAEDG KVIPVTVVQA GPCYVLQKKT EASDGYNAIQ VGFDEKRENL
ATKPEKGHFK KSGVKFMRFI KEFRTAEADS FEVGQEIKAD IFAAGDKVDV VGTSKGKGFA
GMHKRHGARR GPMGHGSKYH HRTGSMGAKG PARVFKGRNL PGRMGGERVT VQNLEVVRVD
TDKNYILIRG CVPGAKKSLL ILKESVKAK
//
