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Database: UniProt
Entry: A0A0B4C0A5_9RHOB
LinkDB: A0A0B4C0A5_9RHOB
Original site: A0A0B4C0A5_9RHOB 
ID   A0A0B4C0A5_9RHOB        Unreviewed;       241 AA.
AC   A0A0B4C0A5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|ARBA:ARBA00035243, ECO:0000256|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN   ORFNames=RA29_18275 {ECO:0000313|EMBL:KIC48131.1};
OS   Tateyamaria sp. ANG-S1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tateyamaria.
OX   NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC48131.1, ECO:0000313|Proteomes:UP000031171};
RN   [1] {ECO:0000313|Proteomes:UP000031171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325}.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIC48131.1}.
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DR   EMBL; JWLL01000009; KIC48131.1; -; Genomic_DNA.
DR   RefSeq; WP_039688641.1; NZ_JWLL01000009.1.
DR   AlphaFoldDB; A0A0B4C0A5; -.
DR   STRING; 1577905.RA29_18275; -.
DR   OrthoDB; 9806135at2; -.
DR   Proteomes; UP000031171; 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; 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.
PE   3: Inferred from homology;
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_01325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031171};
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325}.
FT   MOD_RES         151
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   241 AA;  25769 MW;  A1DEFE2D0BAAABA1 CRC64;
     MRSGILAKKV GMTRLFMEDG KQVPVTVLQL DALQVVGQRT SDKDGYTAVT LGAGTPKVKR
     VSKAMRGHFA AQKVEPKRKL VEFRVTEDNM IDVGEEIIAD HYFEGQFVDV TGTSIGKGFA
     GAMKRHNFGG LRASHGVSIS HRSHGSTGQC QDPGKVFKGK KMAGHMGAAK VTTQNLQVVR
     TDSDRGLIMI KGAVPGSKGG WVTVKDAVKK PFPQNAVLPA ALRSAQKAEP AADEATKEGD
     E
//
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