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Database: UniProt
Entry: A0A1Y6E7J3_9SPHN
LinkDB: A0A1Y6E7J3_9SPHN
Original site: A0A1Y6E7J3_9SPHN 
ID   A0A1Y6E7J3_9SPHN        Unreviewed;       275 AA.
AC   A0A1Y6E7J3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SAMN06297468_0170 {ECO:0000313|EMBL:SMQ58625.1};
OS   Altererythrobacter xiamenensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ58625.1, ECO:0000313|Proteomes:UP000194420};
RN   [1] {ECO:0000313|Proteomes:UP000194420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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   -!- PTM: Methylated by PrmB. {ECO:0000256|HAMAP-Rule:MF_01325}.
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; FXWG01000001; SMQ58625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6E7J3; -.
DR   OrthoDB; 9806135at2; -.
DR   Proteomes; UP000194420; 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   Methylation {ECO:0000256|HAMAP-Rule:MF_01325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194420};
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          228..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   275 AA;  29420 MW;  309D3F213B132F16 CRC64;
     MRTGVIAKKV GMTRLFQEDG RHVPVTVLSL EDCQVVSHRT AERDGYFAVQ LGAGEAKQKN
     VNKPQREAFA KAETGLKKRV AEFRVESEDG LVPVGSTISA EHFVAGQKVD ITGHTQGKGF
     AGAMKRWGFG GLRATHGVSI SHRSHGSTGN RQDPGRVFKG KKMAGHMGDR QRTQQNLEIV
     RTDADRGLIF VKGSVPGSKN GWLLVRDAVK LSAAEDLPFP AAIFDPAAAK PEAEAPAAEE
     QTPVEQDAAP EATDAPAEET KAPEADTGSD ESKES
//
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