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Database: UniProt/SWISS-PROT
Entry: RS4_PELCD
LinkDB: RS4_PELCD
Original site: RS4_PELCD 
ID   RS4_PELCD               Reviewed;         209 AA.
AC   Q3A6M1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-SEP-2014, entry version 56.
DE   RecName: Full=30S ribosomal protein S4;
GN   Name=rpsD; OrderedLocusNames=Pcar_0727;
OS   Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Pelobacteraceae; Pelobacter.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / Gra Bd 1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly to 16S rRNA where it nucleates assembly of the body of
CC       the 30S subunit (By similarity).
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy (By similarity).
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5.
CC       The interaction surface between S4 and S5 is involved in control
CC       of translational fidelity (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR   EMBL; CP000142; ABA87986.1; -; Genomic_DNA.
DR   RefSeq; WP_011340429.1; NC_007498.2.
DR   RefSeq; YP_006716423.1; NC_007498.2.
DR   ProteinModelPortal; Q3A6M1; -.
DR   SMR; Q3A6M1; 2-209.
DR   STRING; 338963.Pcar_0727; -.
DR   EnsemblBacteria; ABA87986; ABA87986; Pcar_0727.
DR   GeneID; 3723316; -.
DR   KEGG; pca:Pcar_0727; -.
DR   PATRIC; 22887454; VBIPelCar86875_0796.
DR   eggNOG; COG0522; -.
DR   HOGENOM; HOG000221003; -.
DR   KO; K02986; -.
DR   OMA; TCKLSRR; -.
DR   OrthoDB; EOG6N3CXM; -.
DR   BioCyc; PCAR338963:GKDU-821-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:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1050.10; -; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR005709; Ribosomal_S4_bac-type.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1    209       30S ribosomal protein S4.
FT                                /FTId=PRO_0000228909.
FT   DOMAIN       98    159       S4 RNA-binding.
SQ   SEQUENCE   209 AA;  24308 MW;  91AA27AEA7BFF5E3 CRC64;
     MARYTGPVCR LCRRETMKLF LKGDRCYTDK CALERRNYAP GQHGQGRTKV SDYGTQLREK
     QRMKRTYGLL EKQFRAYFDK ADSMKGVTGE NLLVLLERRL DSAVYRLGFA SSRTEGRALV
     RQGHFLVNGR KVNIPSYVMR PNDVIELREK SRKITRINDA LDGVMRRGLP SWVELDREAF
     KGTFKTLPVR EEMTTPAFQE QLIVELYSK
//
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