| Protein: | DEF1B_ARATH |
| Organism: | Arabidopsis thaliana |
| Length: | 273 amino acids |
| Reference: | Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for DEF1B_ARATH.
| Description | E-value | Query Range |
Subject Range |
|
|
380.0 | [0..1] | [273..1] |
|
Region A: Residues: [1-273] |
1 11 21 31 41 51
| | | | | |
1 MAVCNCFLQA PPLSRILLPV LSRRATTLSA GYGRLKSTVT FCSTVNRTSP LTSSVRAEVK 60
61 RVSRKDDKVA SATDVQFETP LKIVEYPDPI LRAKNKRIDI FDENLKNLVD AMFDVMYKTD 120
121 GIGLSAPQVG LNVQLMVFNP AGEPGEGKEI VLVNPKIKKY SDKLVPFDEG CLSFPGIYAE 180
181 VVRPQSVKID ARDITGERFS ISLSRLPARI FQHEYDHLEG VLFFDRMTDQ VLDSIREELE 240
241 ALEKKYEEKT GLPSPERVEA RQKRKAGVGF GKR
|
| Detection Method: |  |
| Confidence: | 70.0 |
| Match: | 1ix1A |
| Description: | Crystal Structure of P.aeruginosa Peptide deformylase Complexed with Antibiotic Actinonin |
Matching Structure (courtesy of the PDB): |
|
| Term | Confidence | Notes |
| catalytic activity | 2.58820956037645 | bayes_pls_golite062009 |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | 2.29341894440799 | bayes_pls_golite062009 |
| peptide deformylase activity | 2.09701270257336 | bayes_pls_golite062009 |
| hydrolase activity | 1.74603757697733 | bayes_pls_golite062009 |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 1.59643176725105 | bayes_pls_golite062009 |
| formylmethionine deformylase activity | 0.90550535791718 | bayes_pls_golite062009 |
