Table 2.
General characteristics of Culex quinquefasciatus trypsin-like serine peptidases identified by mass spectrometry ∆
| Uniprot accession number | Protein name | Active sitetriad position | Cysteine pair residues | Residues confering substrate specificity | Protein size (aa) | Activation site | Conserved regions | |||
|---|---|---|---|---|---|---|---|---|---|---|
| Precursor | Mature | LTAAHC | DIAL | GDSGGP | ||||||
| B0WIS4 | Trypsin 1 | His88, Asp133, Ser229 | 73-89, 198-214, 225-249 | Asp223, Gly246,Gly256 | 274 | 226 | YR^IVGG | LTAAHC | DYSL | GDSGGP |
| B0WE94 | Trypsin 2 | His75, Asp120, Ser216 | 60-76, 183-200, 212-236 | Asp210, Gly234,Gly244 | 261 | 226 | GK^IVGG | LTAAHC | DFCL | GDSGGP |
| B0XCW2 | Trypsin 4 | His70, Asp116, Ser213 | 151-219, 181-198, 209-233 | Asp207, Gly230,Gly240 | 258 | 233 | FH^IVNG | LTAAHL | DFAL | GDSGGP |
| B0X667 | Trypsin 5 | His73, Asp127, Ser221 | 58-74, 160-227, 192-208, 217-241 | Asp215, Gly238,Gly248 | 293 | 268 | PK^IIGG | LTAAHC | DIAL | GDSGGP |
| B0XES8 | Trypsin 7 | His67, Asp112, Ser207 | 52-68, 146-213, 176-192, 203-227 | Asp201, Gly224,Gly234 | 252 | 229 | SR^IVNG | LTAGHC | DYAL | GDSGGP |
| B0X870 | SP24D | His63, Asp109, Ser195 | 48-64, 172-181, 191-216 | ? | 240 | 217 | RR^IFGG | LTAAHC | DIAL | GDSGGP |
| B0W9S9 | Serine protease 1/2 | His92, Asp135, Ser233 | 77-93, 202-217, 229-259 | ? | 283 | 235 | SR^IVNG | LTAAHC | DIGL | GDSGGP |
| B0WW44 | Cationic trypsin | His69, Asp114, Ser202 | 54-70 | ? | 244 | 216 | GR^VVGG | LTAGHC | DIAV | YDGGSP |
∆ Extracted after CLUSTAL Omega aligment analysis
(aa) total number of amino acid residues
? = other residues different than DGG
^ = Indicates the clivage site for zymogen activation