(data stored in ACNUC7421 zone)

SWISSPROT: RL3_PSEHT

ID   RL3_PSEHT               Reviewed;         211 AA.
AC   Q3IF25;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 76.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325};
GN   OrderedLocusNames=PSHAa0144;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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 universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
DR   EMBL; CR954246; CAI85248.1; -; Genomic_DNA.
DR   RefSeq; WP_011326865.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF25; -.
DR   STRING; 326442.PSHAa0144; -.
DR   PRIDE; Q3IF25; -.
DR   EnsemblBacteria; CAI85248; CAI85248; PSHAa0144.
DR   GeneID; 32565965; -.
DR   KEGG; pha:PSHAa0144; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   OrthoDB; POG091H009A; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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;
DR   PRODOM; Q3IF25.
DR   SWISS-2DPAGE; Q3IF25.
KW   Complete proteome; Methylation; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1    211       50S ribosomal protein L3.
FT                                /FTId=PRO_0000241388.
FT   MOD_RES     152    152       N5-methylglutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01325}.
SQ   SEQUENCE   211 AA;  22182 MW;  45922A9DBD08011B CRC64;
     MALGLVGRKV GMTRIFTEDG VSIPVTVIEA TPNRIAQIKS EATDGYNALQ VTAGTKKASR
     VNKASAGHFA KAGVEAGRGL WEFRLNGGEG DFEVGAELTV ELFNEINKVD VTGTSKGKGF
     QGGVKRWNFS MQDATHGNSL SHRAPGSIGQ NQSPGKVFKG KKMAGHMGAE RVTTQNLELV
     RVDAERNLLL VKGAVPGAIG GDVIVKPAVK A
//

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