ID A0A1H8SCP4_9BACI Unreviewed; 210 AA.
AC A0A1H8SCP4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN ORFNames=SAMN04488134_11287 {ECO:0000313|EMBL:SEO76345.1};
OS Amphibacillus marinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=872970 {ECO:0000313|EMBL:SEO76345.1, ECO:0000313|Proteomes:UP000199300};
RN [1] {ECO:0000313|EMBL:SEO76345.1, ECO:0000313|Proteomes:UP000199300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10434 {ECO:0000313|EMBL:SEO76345.1,
RC ECO:0000313|Proteomes:UP000199300};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FODJ01000012; SEO76345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8SCP4; -.
DR STRING; 872970.SAMN04488134_11287; -.
DR OrthoDB; 9806135at2; -.
DR Proteomes; UP000199300; Unassembled WGS sequence.
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:UP000199300};
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 113..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 22708 MW; D502434EDB3B0A8C CRC64;
MTKGILGRKV GMTQIFTETG ELIPVTVVQA EPNVVLQKRT LENDGYEAIQ VGFADQKEVN
ANKPSKGHAA KASTTPKRFI REFRNVNLDE YEVGQELSVE VFQAGDVIDA TGTSKGKGFQ
GSIKRHNQQR GPMSHGSHYH RGPGSMGAAA EPARVMKGKK LPGHMGSETT TVQNLEVVKV
DAERNLLLIK GNVPGSKKSF VKITSAIKAN
//
