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Database: UniProt
Entry: Q2S912
LinkDB: Q2S912
Original site: Q2S912 
ID   RL3_HAHCH               Reviewed;         212 AA.
AC   Q2S912;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   01-OCT-2014, entry version 54.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325};
GN   OrderedLocusNames=HCH_06217;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly near the 3'-end of the 23S rRNA, where it nucleates
CC       assembly of the 50S 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 ribosomal protein L3P family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; CP000155; ABC32862.1; -; Genomic_DNA.
DR   RefSeq; YP_437287.1; NC_007645.1.
DR   ProteinModelPortal; Q2S912; -.
DR   SMR; Q2S912; 3-212.
DR   STRING; 349521.HCH_06217; -.
DR   EnsemblBacteria; ABC32862; ABC32862; HCH_06217.
DR   GeneID; 3840207; -.
DR   KEGG; hch:HCH_06217; -.
DR   PATRIC; 22092626; VBIHahChe29232_5653.
DR   eggNOG; COG0087; -.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; SMQDATH; -.
DR   OrthoDB; EOG6WDSMH; -.
DR   BioCyc; HCHE349521:GHAL-6007-MONOMER; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
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.
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   Complete proteome; Methylation; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1    212       50S ribosomal protein L3.
FT                                /FTId=PRO_0000241352.
FT   MOD_RES     153    153       N5-methylglutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01325}.
SQ   SEQUENCE   212 AA;  22207 MW;  025A70B21D3F1433 CRC64;
     MAIGLVGRKA GMTRLFEDDG AAVPVTVIQV EKNVIAQVKS LEVDGYRAIQ VTSGSVKASR
     VNKPMAGHFA KAGVEAGRVV CEFTLDATDS AEYKVGDEVS VTIFEAGQKV DVSGRSKGKG
     FAGVIKRWNF STQDATHGNS LSHRAPGSIG QNQSPGRVFK GKKMAGQMGN KNVTVQTLKV
     VRVDEEKGLL LIKGAVPGAT GADVVIKPAV KA
//
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