| Accession |
MF_01307 |
| Dates |
3-DEC-2002 (Created) 30-JUN-2008 (Last updated, Version 27) |
case <OC:Bacteria> or <OG:Chloroplast>
end case
case <OC:Archaea>
end case
case <OC:Bacteria> and not <OC:Cyanobacteria>
| Protein name |
| RecName: |
Full=30S ribosomal protein S5; |
|
else case <OC:Cyanobacteria>
| Protein name |
| RecName: |
Full=30S ribosomal protein S5; |
|
else case <OC:Archaea>
| Protein name |
| RecName: |
Full=30S ribosomal protein S5P; |
|
else case <OG:Chloroplast>
| Protein name |
| RecName: |
Full=30S ribosomal protein S5, chloroplastic; |
|
end case
FUNCTION: With S4 and S12 plays an important role in translational accuracy (By similarity).
case <OC:Bacteria>
FUNCTION: Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body (By similarity).
SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and S8 (By similarity).
else case <OC:Archaea>
SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4 (By similarity).
else case <OG:Chloroplast>
SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4 (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
DOMAIN: The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
SIMILARITY: Belongs to the ribosomal protein S5P family.
case <Feature:PS50881>
SIMILARITY: Contains 1 S5 DRBM domain.
end case
case <OG:Chloroplast>
end case
case <OC:Bacteria>
| Size range: |
146-254 amino acids |
end case
case <OC:Archaea>
| Size range: |
197-236 amino acids |
end case
| Related UniRules: |
None |
| Template: |
P02357 (RS5_BACST); P21467 (RS5_BACSU); P0A7W1 (RS5_ECOLI); P0A7W4 (RS5_SALTY); Q5SHQ5 (RS5_THET8): [Recover all] |
| Scope: |
Bacteria
Archaea
Plastid |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
in LEPBL |
| Plasmid encoded: |
None |
| Comments: |
CARRP and CENSY are fairly different, made atypical. |
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