AC MF_01306; DC Protein; auto c? or TR HAMAP; MF_01306_B; -; 1; level=0 c? TR HAMAP; MF_01306_A; -; 1; level=0 XX Names: Ribosomal_uS4 XX case and not ID RS4 DE RecName: Full=Small ribosomal subunit protein uS4; GN Name=rpsD; else case ID RS4 DE RecName: Full=Small ribosomal subunit protein uS4; GN Name=rpsD; Synonyms=rps4; else case ID RS4 DE RecName: Full=Small ribosomal subunit protein uS4; GN Name=rps4; else case ID RR4 DE RecName: Full=Small ribosomal subunit protein uS4c; GN Name=rps4; end case XX CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The CC interaction surface between S4 and S5 is involved in control of CC translational fidelity. case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family. XX DR Pfam; PF00163; Ribosomal_S4; 1; trigger=no DR Pfam; PF01479; S4; 1; trigger=no DR NCBIfam; TIGR01018; RpsD_arch; 1; trigger=no DR NCBIfam; TIGR01017; RpsD_bact; 1; trigger=no DR PROSITE; PS00632; RIBOSOMAL_S4; 1; trigger=no DR PROSITE; PS50889; S4; 1; trigger=yes XX KW Ribonucleoprotein KW Ribosomal protein KW RNA-binding KW rRNA-binding XX GO GO:0019843; F:rRNA binding GO GO:0006412; P:translation case GO GO:0009507; C:chloroplast end case XX FT None XX case Size: 192-257; end case case Size: 159-219; end case Related: None; Template: P81288; P21466; P0A7V8; O54297; P80373; P48270; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: None Duplicate: in ALKMQ, ALKOO, AZOSB, BDEBA, CLOAB, CLOB1, CLOBH, CLOBL, CLONN, CLOP1, CLOPE, CLOPS, LEPBL, METFK, NITEU, MYXXD, PSYIN, SYMTH Plasmid: None Comments: Some plastid-encoded rps4 sequences (EIMTE, HELSJ, STIHE, TOXGO), as well as CARRP and NEOSM are quite divergent and thus have been made atypical. The second and third copies in the Clostridia have also been made atypical. In AZOSB the second copy is truncated and probably not functional. XX # Revision 1.36 2023/09/22 //