(data stored in ACNUC7421 zone)

SWISSPROT: D6XVP1_BACIE

ID   D6XVP1_BACIE            Unreviewed;       208 AA.
AC   D6XVP1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000256|HAMAP-Rule:MF_01325, ECO:0000256|RuleBase:RU003906};
GN   Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN   OrderedLocusNames=Bsel_0115 {ECO:0000313|EMBL:ADH97664.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97664.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97664.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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:0000256|HAMAP-Rule:MF_01325,
CC       ECO:0000256|RuleBase:RU003906}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325,
CC       ECO:0000256|RuleBase:RU003906}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01325, ECO:0000256|RuleBase:RU003905}.
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DR   EMBL; CP001791; ADH97664.1; -; Genomic_DNA.
DR   RefSeq; WP_013171094.1; NC_014219.1.
DR   STRING; 439292.Bsel_0115; -.
DR   EnsemblBacteria; ADH97664; ADH97664; Bsel_0115.
DR   KEGG; bse:Bsel_0115; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   OrthoDB; 1270636at2; -.
DR   BioCyc; BSEL439292:G1GLR-139-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XVP1.
DR   SWISS-2DPAGE; D6XVP1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003905};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003905, ECO:0000313|EMBL:ADH97664.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003906};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW   ECO:0000256|RuleBase:RU003906}.
SQ   SEQUENCE   208 AA;  22532 MW;  6CF865073458788F CRC64;
     MTKGILGKKL GMTQIFSENG EQVPVTVIEA SPNVVLQKKT AEGEGYEAIQ IGYDDKKANR
     QNSPEKGHAE KAKTAPKRFV KEIRDVNTAD YEIGQEIKVD IFAEGDAIDV TGTSKGKGFQ
     GAIKRHNQSR GPMSHGSRYH RRPGSMGPVD PNHVRPGKLL PGQMGGETVT IQNLEVVKVD
     TERNVILVKG NVPGARKSFV TITSATKA
//

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