| Accession | TIGR00475 |
| Name | selB |
| Function | selenocysteine-specific translation elongation factor |
| Gene Symbol | selB |
| Trusted Cutoff | 242.25 |
| Domain Trusted Cutoff | 242.25 |
| Noise Cutoff | 229.00 |
| Domain Noise Cutoff | 229.00 |
| Isology Type | equivalog |
| HMM Length | 581 |
| Mainrole Category | Protein synthesis |
| Subrole Category | Translation factors |
| Gene Ontology Term | GO:0001514: selenocysteine incorporation biological_process |
| | GO:0003746: translation elongation factor activity molecular_function |
| | GO:0006414: translational elongation biological_process |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:09PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This HMM describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. |
| References | SE TIGR
RM 12486046
RT Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs.
RA Rother M, Mathes I, Lottspeich F, Bock A.
RL J Bacteriol. 2003 Jan;185(1):107-14. |
| Genome Property | GenProp0016: selenocysteine system (HMM) |
