(data stored in ACNUC7421 zone)

SWISSPROT: RL3_POLNA

ID   RL3_POLNA               Reviewed;         226 AA.
AC   A1VIQ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 66.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Pnap_0203;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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}.
DR   EMBL; CP000529; ABM35528.1; -; Genomic_DNA.
DR   RefSeq; WP_011799637.1; NC_008781.1.
DR   SMR; A1VIQ0; -.
DR   STRING; 365044.Pnap_0203; -.
DR   EnsemblBacteria; ABM35528; ABM35528; Pnap_0203.
DR   KEGG; pna:Pnap_0203; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000000644; Chromosome.
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   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03625; L3_bact; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1VIQ0.
DR   SWISS-2DPAGE; A1VIQ0.
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..226
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000052104"
FT   MOD_RES         158
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   226 AA;  23608 MW;  1506BD94BAB718C0 CRC64;
     MSLSNSLGLL GRKVGMMRLF TDDGDTVPVT VVDVSNNRVT QVKTEANDGY DALQVAFGSR
     KASRVTKPEA GHLAKAGVEA GEILKEFRVT ADVAGKYAAG TVVPAADIFA VGQLVDVQGT
     SIGKGFAGTI KRHKMSSQRA SHGNSRSHNV PGSIGMAQDP GRVFPGKRMT GHLGDVTKTT
     QNLDIVRIDE ARQLLMIRGA VPGSKGGFVT VRAAIKAKPT AAKGAN
//

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