(data stored in ACNUC7421 zone)

HOGENOM: THEFY_1_PE1011

ID   THEFY_1_PE1011                       STANDARD;      PRT;   203 AA.
AC   THEFY_1_PE1011; Q47R66;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=30S ribosomal protein S4; (THEFY_1.PE1011).
GN   Name=rpsD; OrderedLocusNames=Tfu_1013;
OS   THERMOBIFIDA FUSCA YX.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEFY_1.PE1011.
CC       Thermobifida fusca YX, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:RS4_THEFY
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.
CC   -!- GENE_FAMILY: HOG000221004 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q47R66; -.
DR   EMBL; CP000088; AAZ55051.1; -; Genomic_DNA.
DR   RefSeq; YP_289074.1; NC_007333.1.
DR   ProteinModelPortal; Q47R66; -.
DR   STRING; Q47R66; -.
DR   GeneID; 3579273; -.
DR   GenomeReviews; CP000088_GR; Tfu_1013.
DR   KEGG; tfu:Tfu_1013; -.
DR   NMPDR; fig|269800.4.peg.1105; -.
DR   eggNOG; COG0522; -.
DR   OMA; VMEPNLV; -.
DR   ProtClustDB; PRK05327; -.
DR   BioCyc; TFUS269800:TFU_1013-MON; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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_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; IPR018079; Ribosomal_S4_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   Gene3D; G3DSA:1.10.1050.10; G3DSA:1.10.1050.10; 1.
DR   Gene3D; G3DSA:3.10.290.10; G3DSA:3.10.290.10; 1.
DR   PANTHER; PTHR11831; Ribosomal_S4; 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; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
DR   HOGENOMDNA; THEFY_1.PE1011; -.
KW   30S ribosomal protein S4;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
SQ   SEQUENCE   203 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRYTGPKVRL SRRAGVPLTR KAVKYFEKRP YPPGEHGRRV RRSTSDYAVR QAEKQKLRWY
     YDLSEKQLAR VYENAKKRPG RTGEEMIAEL ELRLATVLLR AGFAASIYAA RQFINHGHIT
     VDGKKVDIPS YQVKPGQIVS VREKSRKLVP FIEAAEGVHA DEKIASYLAV SHKDLTIAVV
     DRPKREQVPV PFDEQLVVEY YAR
//

If you have problems or comments...

PBIL Back to PBIL home page