You are browsing environment: FUNGIDB
CAZyme Information: ASPVEDRAFT_188663-t33_1-p1
You are here: Home > Sequence: ASPVEDRAFT_188663-t33_1-p1
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Aspergillus versicolor | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor | |||||||||||
| CAZyme ID | ASPVEDRAFT_188663-t33_1-p1 | |||||||||||
| CAZy Family | PL4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | ||||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 173788 | Peptidases_S53 | 1.45e-122 | 214 | 584 | 2 | 355 | Peptidase domain in the S53 family. Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase. |
| 401284 | Pro-kuma_activ | 4.63e-47 | 40 | 180 | 2 | 142 | Pro-kumamolisin, activation domain. Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide. |
| 206778 | Pro-peptidase_S53 | 1.15e-40 | 40 | 177 | 1 | 139 | Activation domain of S53 peptidases. Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase. |
| 214928 | Pro-kuma_activ | 1.18e-30 | 46 | 178 | 5 | 136 | Pro-kumamolisin, activation domain. This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase. |
| 227270 | COG4934 | 5.44e-29 | 57 | 589 | 52 | 552 | Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 597 | 1077 | 6 | 488 | |
| 2.20e-93 | 665 | 1077 | 82 | 477 | |
| 2.20e-93 | 665 | 1077 | 82 | 477 | |
| 3.06e-93 | 665 | 1077 | 82 | 477 | |
| 3.06e-93 | 665 | 1077 | 82 | 477 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 8.36e-68 | 32 | 591 | 7 | 539 | Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1 [Homo sapiens] |
|
| 1.55e-67 | 32 | 591 | 26 | 558 | Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens],3EE6_B Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens] |
|
| 7.19e-26 | 350 | 602 | 122 | 364 | Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SIO_B Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SIO_C Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SN7_A Kumamolisin-As, Apoenzyme [Alicyclobacillus sendaiensis] |
|
| 7.19e-26 | 350 | 602 | 122 | 364 | Chain A, kumamolisin-As [Alicyclobacillus sendaiensis] |
|
| 1.76e-25 | 350 | 602 | 122 | 364 | Chain A, kumamolisin [Bacillus sp. MN-32] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7.52e-272 | 1 | 600 | 1 | 596 | Tripeptidyl-peptidase sed3 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=sed3 PE=1 SV=1 |
|
| 5.61e-199 | 20 | 595 | 26 | 600 | Tripeptidyl-peptidase SED4 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED4 PE=3 SV=1 |
|
| 3.61e-198 | 27 | 596 | 26 | 595 | Tripeptidyl-peptidase SED3 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED3 PE=3 SV=1 |
|
| 2.97e-196 | 31 | 596 | 27 | 592 | Probable tripeptidyl-peptidase SED3 OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=SED3 PE=3 SV=2 |
|
| 2.97e-196 | 31 | 596 | 27 | 592 | Probable tripeptidyl-peptidase SED3 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=SED3 PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000517 | 0.999477 | CS pos: 23-24. Pr: 0.9826 |