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Database: UniProt/TrEMBL
Entry: F8FA29_PAEMK
LinkDB: F8FA29_PAEMK
Original site: F8FA29_PAEMK 
ID   F8FA29_PAEMK            Unreviewed;       165 AA.
AC   F8FA29;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   14-MAY-2014, entry version 18.
DE   RecName: Full=30S ribosomal protein S5;
GN   Name=rpsE; OrderedLocusNames=KNP414_07508;
OS   Paenibacillus mucilaginosus (strain KNP414).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1036673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414;
RA   Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Located at the back of the 30S subunit body where it
CC       stabilizes the conformation of the head with respect to the body
CC       (By similarity).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy (By similarity).
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4
CC       and S8 (By similarity).
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and
CC       contacts protein S4. The interaction surface between S4 and S5 is
CC       involved in control of translational fidelity (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC   -!- SIMILARITY: Contains 1 S5 DRBM domain.
CC   -!- SIMILARITY: Contains S5 DRBM domain.
CC   -!- SIMILARITY: Contains SDRBM domain.
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DR   EMBL; CP002869; AEI46002.1; -; Genomic_DNA.
DR   RefSeq; YP_004645872.1; NC_015690.1.
DR   EnsemblBacteria; AEI46002; AEI46002; KNP414_07508.
DR   GeneID; 10860387; -.
DR   KEGG; pms:KNP414_07508; -.
DR   KO; K02988; -.
DR   OMA; PAHEGTG; -.
DR   BioCyc; PMUC1036673:GJD1-7511-MONOMER; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR014720; dsRNA-bd_dom.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   DOMAIN       10     73       S5 DRBM (By similarity).
SQ   SEQUENCE   165 AA;  17169 MW;  42551CFA1470854A CRC64;
     MRIDPNTLEL SEKVVQINRV AKVVKGGRRF SFSALVVVGD GNGWVGAGIG KASEVPDAIR
     KGIEDAKKNL IHVPIVGTTI PHLVTGKFGA GQVLLKPASK GTGVIAGGPV RAVLELAGVG
     DILTKSLGSS NSMNMVNATL EGLQRLKRAE DVAKLRGKTV EELLG
//
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