| Accession | TIGR00293 |
| Name | TIGR00293 |
| Function | prefoldin, alpha subunit |
| Gene Symbol | pfdA |
| Trusted Cutoff | 53.90 |
| Domain Trusted Cutoff | 53.90 |
| Noise Cutoff | 43.00 |
| Domain Noise Cutoff | 43.00 |
| Isology Type | equivalog |
| HMM Length | 129 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein folding and stabilization |
| Gene Ontology Term | GO:0005515: protein binding molecular_function |
| | GO:0006457: protein folding biological_process |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:05PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model.
This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and builds of HMMs for the seed alignment with less selective parameters lead to significant hits to large numbers of proteins that contain coiled coil regions. This model is built with a more selective usage of Dirichlet priors. |
| References | SE TIGR
AL clustalw, belvu
DR HAMAP; MF_00308; 48 of 48 |
| Genome Property | GenProp0246: chaperone system: thermosome/prefoldin (HMM) |
