| Protein: | DPP1 |
| Organism: | Saccharomyces cerevisiae |
| Length: | 289 amino acids |
| Reference: | Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for DPP1.
| Description | E-value | Query Range |
Subject Range |
|
|
7.0E-63 | [13..283] | [1..285] |
|
|
4.0E-62 | [13..283] | [1..285] |
|
|
8.0E-60 | [13..283] | [1..283] |
|
|
2.0E-56 | [1..289] | [1..289] |
|
|
6.0E-55 | [6..288] | [65..347] |
|
|
2.0E-54 | [6..259] | [60..306] |
|
Region A: Residues: [1-60] |
1 11 21 31 41 51
| | | | | |
1 MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL TISHPYATTE 60
61
|
| Detection Method: |  |
Shown below are all of our de novo (Rosetta) predictions for this domain.
Click here to view only most confident match.
| MCM Score |
GO Score |
GO Term |
SCOP Match |
SCOP Description | ||
| View | Download | 0.458 | 0.926 | phospholipid metabolic process | c.2.1 | NAD(P)-binding Rossmann-fold domains |
| View | Download | 0.458 | 0.926 | phospholipid metabolic process | c.2.1 | NAD(P)-binding Rossmann-fold domains |
| View | Download | 0.452 | 0.926 | phospholipid metabolic process | g.18.1 | Complement control module/SCR domain |
| View | Download | 0.246 | 0.926 | phospholipid metabolic process | c.30.1 | PreATP-grasp domain |
| View | Download | 0.256 | 0.926 | phospholipid metabolic process | d.109.1 | Actin depolymerizing proteins |
| View | Download | 0.424 | 0.926 | phospholipid metabolic process | d.68.1 | Translation initiation factor IF3, C-terminal domain |
| View | Download | 0.256 | 0.926 | phospholipid metabolic process | d.109.1 | Actin depolymerizing proteins |
| View | Download | 0.424 | 0.926 | phospholipid metabolic process | d.68.1 | Translation initiation factor IF3, C-terminal domain |
| View | Download | 0.361 | 0.926 | phospholipid metabolic process | c.2.1 | NAD(P)-binding Rossmann-fold domains |
| View | Download | 0.234 | 0.926 | phospholipid metabolic process | g.14.1 | Kringle-like |
| View | Download | 0.230 | 0.926 | phospholipid metabolic process | c.78.1 | Aspartate/ornithine carbamoyltransferase |
| View | Download | 0.215 | 0.926 | phospholipid metabolic process | c.51.1 | Anticodon-binding domain of Class II aaRS |
| View | Download | 0.213 | 0.926 | phospholipid metabolic process | d.88.1 | SRF-like |
| View | Download | 0.212 | 0.926 | phospholipid metabolic process | d.109.1 | Actin depolymerizing proteins |
| View | Download | 0.202 | 0.926 | phospholipid metabolic process | c.102.1 | Cell-division inhibitor MinC, N-terminal domain |
|
Region A: Residues: [61-289] |
1 11 21 31 41 51
| | | | | |
1 RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL LGLSLAWFST SFFTNFIKNW 60
61 IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC TTKNHERLLD GFRTTPSGHS SESFAGLGYL 120
121 YFWLCGQLLT ESPLMPLWRK MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH 180
181 FFYRRIFPPI DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM
|
| Detection Method: | |
| Confidence: | 5.221849 |
| Match: | 1d2tA_ |
| Description: | Bacterial acid phosphatase |
Matching Structure (courtesy of the PDB): |
|
