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CAZyme Information: PHYSODRAFT_487620-t26_1-p1

You are here: Home > Sequence: PHYSODRAFT_487620-t26_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 Phytophthora sojae
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
CAZyme ID PHYSODRAFT_487620-t26_1-p1
CAZy Family GH7
CAZyme Description polygalacturonase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
254 JH159152|CGC17 26471.34 7.2102
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PsojaeP6497 28142 1094619 1653 26489
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.15:10

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH28 1 247 1.7e-57 0.7046153846153846

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 6.91e-54 1 242 63 308
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 2.96e-23 1 215 153 370
Probable polygalacturonase
177865 PLN02218 4.77e-23 1 223 168 391
polygalacturonase ADPG
227721 Pgu1 1.98e-22 1 218 209 459
Polygalacturonase [Carbohydrate transport and metabolism].
215540 PLN03010 4.80e-22 1 223 149 357
polygalacturonase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.26e-150 1 252 110 361
1.30e-148 1 254 138 391
1.30e-148 1 254 138 391
7.75e-143 1 252 138 389
6.65e-141 1 252 219 470

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.19e-44 1 237 80 319
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]
5.44e-43 1 241 88 330
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
5.44e-43 1 241 88 330
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
1.36e-41 1 241 80 322
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
3.09e-39 1 242 80 323
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
1.25e-45 1 237 107 346
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
1.27e-44 1 242 105 346
Polygalacturonase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PGU1 PE=1 SV=1
7.09e-44 1 237 105 342
Probable endopolygalacturonase B OS=Aspergillus kawachii OX=1069201 GN=pgaB PE=3 SV=1
1.43e-43 1 242 108 350
Probable endopolygalacturonase A OS=Aspergillus parasiticus OX=5067 GN=pgaA PE=2 SV=1
1.47e-43 1 252 126 378
Endo-polygalacturonase OS=Sclerotinia sclerotiorum OX=5180 GN=PG1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000016 0.000009

TMHMM  Annotations      help

There is no transmembrane helices in PHYSODRAFT_487620-t26_1-p1.