| Accession | TIGR00731 |
| Name | bL25_bact_ctc |
| Function | ribosomal protein bL25, Ctc-form |
| Trusted Cutoff | 73.10 |
| Domain Trusted Cutoff | 73.10 |
| Noise Cutoff | 70.35 |
| Domain Noise Cutoff | 70.35 |
| Isology Type | equivalog |
| HMM Length | 176 |
| Mainrole Category | Protein synthesis |
| Subrole Category | Ribosomal proteins: synthesis and modification |
| Gene Ontology Term | GO:0000315: organellar large ribosomal subunit cellular_component |
| | GO:0003735: structural constituent of ribosome molecular_function |
| | GO:0006412: translation biological_process |
| | GO:0006950: response to stress biological_process |
| | GO:0008097: 5S rRNA binding molecular_function |
| | GO:0022625: cytosolic large ribosomal subunit cellular_component |
| Author | Haft DH |
| Entry Date | Feb 22 2000 11:31AM |
| Last Modified | Sep 4 2014 11:49AM |
| Comment | This HMM models a family of proteins with full-length homology to the general stress protein Ctc of Bacillus subtilis, a mesophile, and ribosomal protein TL5 of Thermus thermophilus, a thermophile. Ribosomal protein L25 of Escherichia coli and H. influenzae appear to be orthologous but consist only of the N-terminal half of Ctc and TL5. Both short (L25-like) and full-length (CTC-like) members of this family bind the E-loop of bacterial 5S rRNA. This protein appears to be restricted to bacteria and organelles, and consists of at most one copy per prokaryotic genome.Ctc of Bacillus subtilis has now been localized to ribosomes and can be viewed as the long form, or Ctc form, of L25.
The C-terminal domain of sll1824, an apparent L25 of Synechocystis PCC6803, matches the N-terminal domain of this family. Examples of L25 and Ctc are not separated by a UPGMA tree built on the region of shared homology. |
| References | AL clustalw_manual
RN [1]
RM 12432960
RT The general stress protein Ctc of Bacillus subtilis is a ribosomal protein.
RA Schmalisch M, Langbein I, Stulke J.
RL J Mol Microbiol Biotechnol. 2002 Sep;4(5):495-501.
RN [2]
RM 99283874
RN [3]
RM 99016057
DR HAMAP; MF_01334; 297 of 298 |
