You are browsing environment: FUNGIDB
CAZyme Information: PHYCI_261708T0-p1
You are here: Home > Sequence: PHYCI_261708T0-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 | Phytophthora cinnamomi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi | |||||||||||
| CAZyme ID | PHYCI_261708T0-p1 | |||||||||||
| CAZy Family | GH30 | |||||||||||
| CAZyme Description | unspecified product | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 3.2.1.15:10 |
|---|
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395231 | Glyco_hydro_28 | 4.85e-59 | 1 | 273 | 42 | 321 | Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes are important in cell wall metabolism. |
| 215426 | PLN02793 | 4.20e-28 | 8 | 234 | 141 | 370 | Probable polygalacturonase |
| 215540 | PLN03010 | 2.46e-27 | 10 | 242 | 139 | 357 | polygalacturonase |
| 177865 | PLN02218 | 1.64e-26 | 4 | 242 | 150 | 391 | polygalacturonase ADPG |
| 178580 | PLN03003 | 6.12e-24 | 12 | 239 | 115 | 337 | Probable polygalacturonase At3g15720 |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 4.02e-188 | 1 | 273 | 91 | 363 | |
| 2.87e-176 | 1 | 273 | 119 | 391 | |
| 6.17e-159 | 1 | 273 | 200 | 472 | |
| 6.17e-159 | 1 | 273 | 200 | 472 | |
| 5.03e-158 | 1 | 273 | 200 | 472 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.93e-53 | 1 | 273 | 67 | 344 | Chain A, Endo-polygalacturonase [Evansstolkia leycettana] |
|
| 2.93e-53 | 1 | 273 | 67 | 344 | Chain A, endo-polygalacturonase [Evansstolkia leycettana] |
|
| 7.36e-52 | 1 | 273 | 59 | 336 | Chain A, Endo-polygalacturonase [Evansstolkia leycettana] |
|
| 4.83e-50 | 1 | 269 | 59 | 333 | Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_B Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_C Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_D Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_E Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_F Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_G Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini] |
|
| 2.96e-47 | 1 | 273 | 59 | 336 | Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_B Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_C Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_D Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_E Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_F Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 8.12e-54 | 1 | 273 | 86 | 364 | Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1 |
|
| 7.47e-52 | 1 | 273 | 90 | 367 | Probable endopolygalacturonase I OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=pgaI PE=3 SV=1 |
|
| 7.47e-52 | 1 | 273 | 90 | 367 | Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2 |
|
| 7.47e-52 | 1 | 273 | 90 | 367 | Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1 |
|
| 9.54e-52 | 1 | 273 | 87 | 363 | Probable endopolygalacturonase A OS=Aspergillus parasiticus OX=5067 GN=pgaA PE=2 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000030 | 0.000016 |