{PDOC00505}
{PS00585; RIBOSOMAL_S5}
{PS50881; S5_DSRBD}
{BEGIN}
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* Ribosomal protein S5 signature and profile *
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Ribosomal protein S5 is one of the proteins from the  small ribosomal subunit.
In Escherichia  coli, S5 is known to be important in the assembly and function
of the 30S ribosomal subunit.  Mutations  in  S5  have  been shown to increase
translational error frequencies.

The  crystal  structure  of the S5 protein has been solved [1] and consists of
two  separated  domains  (see <PDB:1PKP>). An N-terminal domain which displays
some  structurale  homology  to  the  dsRBD  domain (alpha-beta(3)-alpha) (see
<PDOC50137>)  and  a  mainly helical C-terminal domain that interacts with S8.
The dsRBD domain of the S5 protein interacts with the 16S RNA [2].

S5  belongs  to a family of ribosomal proteins which, on the basis of sequence
similarities [3,4], groups:

 - Eubacterial S5.
 - Cyanelle S5.
 - Red algal chloroplast S5.
 - Archaebacterial S5.
 - Mammalian S2 (LLrep3).
 - Caenorhabditis elegans S2 (C49H3.11).
 - Drosophila S2.
 - Plant S2.
 - Yeast S4 (SUP44).
 - Fungi mitochondrial S5.

S5  is  a protein of 166 to 254 amino-acid residues. The signature pattern for
this  protein is based on a conserved region, rich in glycine residues located
in  the  N-terminal  domain.  The  profile  we  developed  covers  the  entire
N-terminal dsRBD domain.

-Consensus pattern: G-[KRQEA]-x(3)-[FYVIM]-x-[ACVTI]-x(2)-[LIVMA]-[LIVMAT]-
                    [AG]-[DN]-x(2,3)-G-x-[LIVMA]-[GS]-x-[SAG]-x(5,6)-[DEQGHS]-
                    [LIVMARFY]-x(2,3)-[AS]-[LIVMFRY]
-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Ramakrishnan V., White S.W.
     "The structure of ribosomal protein S5 reveals sites of interaction
     with 16S rRNA."
     Nature 358:768-771(1992).
     PubMed=1508272; DOI=10.1038/358768a0
[ 2] Brodersen D.E., Clemons W.M. Jr., Carter A.P., Wimberly B.T.,
     Ramakrishnan V.
     "Crystal structure of the 30 S ribosomal subunit from Thermus
     thermophilus: structure of the proteins and their interactions with 16
     S RNA."
     J. Mol. Biol. 316:725-768(2002).
     PubMed=11866529; DOI=10.1006/jmbi.2001.5359
[ 3] All-Robyn J.A., Brown N., Otaka E., Liebman S.W.
     Mol. Cell. Biol. 10:6544-6553(1990).
[ 4] Otaka E., Hashimoto T., Mizuta K.
     Protein Seq. Data Anal. 5:285-300(1993).

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