HAMAP annotation rule MF_01306
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Accession MF_01306
Dates 3-DEC-2002 (Created)
29-JUN-2012 (Last updated, Version 29)
Name Ribosomal_S4
Scope Bacteria
Archaea
Plastid
case <OC:Bacteria> or <OG:Chloroplast>
Triggered by
end case

case <OC:Archaea>
Triggered by
end case




case <OC:Bacteria> and not <OC:Cyanobacteria>
Identifier
RS4
Protein name
RecName: Full=30S ribosomal protein S4;
Gene name
rpsD
else case <OC:Cyanobacteria>
Identifier
RS4
Protein name
RecName: Full=30S ribosomal protein S4;
Gene name
rpsD, rps4
else case <OC:Archaea>
Identifier
RS4
Protein name
RecName: Full=30S ribosomal protein S4;
Gene name
rps4
else case <OG:Chloroplast>
Identifier
RR4
Protein name
RecName: Full=30S ribosomal protein S4, chloroplastic;
Gene name
rps4
end case


FUNCTION One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (By similarity).
With S5 and S12 plays an important role in translational accuracy (By similarity).
SUBUNIT Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity).
case <OG:Chloroplast>
SUBCELLULAR LOCATION Plastid, chloroplast.
end case
SIMILARITY Belongs to the ribosomal protein S4P family.


Ribonucleoprotein
Ribosomal protein
RNA-binding
rRNA-binding


GO:0019843; Molecular function: rRNA binding.
GO:0006412; Biological process: translation.
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case


Pfam PF00163; Ribosomal_S4; 1;
PF01479; S4; 1;
TIGRFAMs TIGR01018; RpsD_arch; 1;
TIGR01017; RpsD_bact; 1;
PROSITE PS00632; RIBOSOMAL_S4; 1;
PS50889; S4; 1; trigger=PRU00182;


case <OC:Bacteria>
Size range: 192-257 amino acids
end case
case <OC:Archaea>
Size range: 159-219 amino acids
end case
Related Rules: None
Templates: P81288 (RS4_GEOSE); P21466 (RS4_BACSU); P0A7V8 (RS4_ECOLI); O54297 (RS4_SALTY); P80373 (RS4_THET8); P48270 (RR4_CHLRE): [Recover all]
Fusion: 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.


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