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CAZyme Information: PITG_10255-t26_1-p1
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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 infestans | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora infestans | |||||||||||
| CAZyme ID | PITG_10255-t26_1-p1 | |||||||||||
| CAZy Family | GH30 | |||||||||||
| CAZyme Description | polygalacturonase, putative | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 3.2.1.15:10 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH28 | 64 | 367 | 4.2e-61 | 0.9261538461538461 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395231 | Glyco_hydro_28 | 5.54e-73 | 66 | 363 | 1 | 304 | 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. |
| 177865 | PLN02218 | 3.93e-25 | 66 | 348 | 95 | 391 | polygalacturonase ADPG |
| 227721 | Pgu1 | 9.07e-24 | 117 | 305 | 200 | 403 | Polygalacturonase [Carbohydrate transport and metabolism]. |
| 215540 | PLN03010 | 1.39e-22 | 118 | 348 | 141 | 357 | polygalacturonase |
| 215426 | PLN02793 | 1.56e-21 | 66 | 338 | 80 | 370 | Probable polygalacturonase |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 6.59e-219 | 1 | 379 | 1 | 380 | |
| 2.11e-211 | 1 | 379 | 1 | 402 | |
| 4.40e-209 | 1 | 379 | 1 | 414 | |
| 8.87e-209 | 1 | 379 | 1 | 414 | |
| 1.39e-205 | 1 | 379 | 1 | 414 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.80e-70 | 51 | 377 | 11 | 342 | Chain A, Endo-polygalacturonase [Evansstolkia leycettana] |
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| 1.80e-70 | 51 | 377 | 11 | 342 | Chain A, endo-polygalacturonase [Evansstolkia leycettana] |
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| 4.45e-69 | 51 | 377 | 3 | 334 | Chain A, Endo-polygalacturonase [Evansstolkia leycettana] |
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| 5.90e-60 | 66 | 375 | 18 | 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] |
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| 3.00e-59 | 51 | 363 | 3 | 319 | 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 |
|---|---|---|---|---|---|---|
| 4.57e-69 | 51 | 375 | 39 | 372 | Polygalacturonase OS=Penicillium griseoroseum OX=84562 GN=PGG1 PE=3 SV=1 |
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| 1.43e-68 | 66 | 377 | 64 | 378 | Endo-polygalacturonase OS=Sclerotinia sclerotiorum OX=5180 GN=PG1 PE=3 SV=1 |
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| 2.01e-67 | 45 | 367 | 20 | 351 | Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1 |
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| 1.71e-66 | 48 | 367 | 31 | 354 | Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1 |
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| 1.71e-66 | 48 | 367 | 31 | 354 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000227 | 0.999740 | CS pos: 25-26. Pr: 0.6276 |