| Accession | TIGR00010 |
| Name | TIGR00010 |
| Function | hydrolase, TatD family |
| Trusted Cutoff | 206.00 |
| Domain Trusted Cutoff | 206.00 |
| Noise Cutoff | 108.85 |
| Domain Noise Cutoff | 108.85 |
| Isology Type | subfamily |
| HMM Length | 253 |
| Mainrole Category | Unknown function |
| Subrole Category | Enzymes of unknown specificity |
| Gene Ontology Term | GO:0008152: metabolic process biological_process |
| | GO:0016787: hydrolase activity molecular_function |
| Author | Haft DH, Richardson DL, Hickey E |
| Entry Date | Feb 22 2000 11:31AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | PSI-BLAST, starting with a urease alpha subunit, finds a large superfamily of proteins, including a number of different enzymes that act as hydrolases at C-N bonds other than peptide bonds (EC 3.5.-.-), many uncharacterized proteins, and the members of this family.
Several genomes have multiple paralogs related to this family. However, a set of 17 proteins can be found, one each from 17 of the first 20 genomes, such that each member forms a bidirectional best hit across genomes with all other members of the set. This core set (and one other near-perfect member), but not the other paralogs, form the seed for this model. Additionally, members of the seed alignment and all trusted hits, but not all paralogs, have a conserved motif DxHxH near the amino end. The member from E. coli was recently shown to have DNase activity. |
| References | SE TIGR
AL clustalw_manual
RM 10747959
RT TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export.
RA Wexler M, Sargent F, Jack RL, Stanley NR, Bogsch EG, Robinson C, Berks BC, Palmer T.
RL J Biol Chem 2000 Jun 2;275(22):16717-22 |
