ID   RL3_MYCVP               Reviewed;         218 AA.
AC   A1T4N9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Mvan_1305;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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: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   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; CP000511; ABM12139.1; -; Genomic_DNA.
DR   RefSeq; WP_011778570.1; NC_008726.1.
DR   AlphaFoldDB; A1T4N9; -.
DR   SMR; A1T4N9; -.
DR   STRING; 350058.Mvan_1305; -.
DR   EnsemblBacteria; ABM12139; ABM12139; Mvan_1305.
DR   KEGG; mva:Mvan_1305; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_4_1_11; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000009159; 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;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..218
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000052094"
FT   REGION          133..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  23045 MW;  995042873048AFD4 CRC64;
     MARKGILGTK LGMTQVFDEN NKVVPVTVVK AGPNVVTRIR TPERDGYSAV QLAYGEISPR
     KVNKPVTGQY AAAGVNPRRH LAELRLDDEA AAAEYEVGQE LTAEIFADGA YVDVTGTSKG
     KGFAGTMKRH GFRGQGASHG AQAVHRRPGS IGGCATPGRV FKGTRMSGRM GSDRVTTQNL
     KVHKVDAENG VLLIKGAIPG RNGGLVVVRS AIKRGEKA