(data stored in SCRATCH3701 zone)

SWISSPROT: RL3_RICTY

ID   RL3_RICTY               Reviewed;         215 AA.
AC   Q68W78;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=RT0651;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04114.1; -; Genomic_DNA.
DR   RefSeq; WP_011191091.1; NC_006142.1.
DR   SMR; Q68W78; -.
DR   STRING; 257363.RT0651; -.
DR   PRIDE; Q68W78; -.
DR   EnsemblBacteria; AAU04114; AAU04114; RT0651.
DR   KEGG; rty:RT0651; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   OrthoDB; 1270636at2; -.
DR   BioCyc; RTYP257363:G1G0L-656-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68W78.
DR   SWISS-2DPAGE; Q68W78.
KW   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..215
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000241404"
FT   MOD_RES         151
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   215 AA;  23542 MW;  9C080B4C0284A59D CRC64;
     MRTGIIAQKI GMTSVFNDKG ERISLTLVKV DGCQVVGHKT LAKHGYNALV IGVKDQKISR
     VTKPMKQVFA NAKISPKTKL KEFRISEDNF IDIASILEVD HFSVGQFVDI TATTIGKGFA
     GSMKRHNFRG LEASHGVSIS HRSHGSTGQR QDPGKVFKGK KMAGHMGCNQ VTIQNLKIFA
     IDTNRKLIMI QGSIPGHKNS YLLVKDAIKK ASITI
//

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