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Database: UniProt
Entry: A7IFY1
LinkDB: A7IFY1
Original site: A7IFY1 
ID   RL3_XANP2               Reviewed;         241 AA.
AC   A7IFY1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   29-OCT-2014, entry version 47.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325};
GN   OrderedLocusNames=Xaut_1679;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000781; ABS66924.1; -; Genomic_DNA.
DR   RefSeq; YP_001416581.1; NC_009720.1.
DR   ProteinModelPortal; A7IFY1; -.
DR   STRING; 78245.Xaut_1679; -.
DR   EnsemblBacteria; ABS66924; ABS66924; Xaut_1679.
DR   GeneID; 5424568; -.
DR   KEGG; xau:Xaut_1679; -.
DR   PATRIC; 24045389; VBIXanAut29526_1990.
DR   eggNOG; COG0087; -.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; SMQDATH; -.
DR   OrthoDB; EOG6WDSMH; -.
DR   BioCyc; XAUT78245:GHS6-1694-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    241       50S ribosomal protein L3.
FT                                /FTId=PRO_1000141943.
FT   MOD_RES     151    151       N5-methylglutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01325}.
SQ   SEQUENCE   241 AA;  25450 MW;  C8C1F8597721CD85 CRC64;
     MRSGVIAQKV GMTRIFTDAG EHVPVTVLKV ESCQVVAHRT LDKNGYVAVQ LGAGRRKPKN
     VTRAERGHFA VAQVEPKHKL AEFRVPEEAL IPVGAEITAD HFVVGQYVDV TGTTIGKGFA
     GGMKRHNFGG LRATHGVSIS HRSIGSTGGR QDPGKTFKNK KMPGHMGDVT VTTQNLKVVM
     TDVERGLIAV EGAVPGHAGG WITVRDAVKK KLPAEAPKPG AFKLNGSEAA PAAEAVNEEG
     A
//
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