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CAZyme Information: PHYSODRAFT_259959-t26_1-p1

You are here: Home > Sequence: PHYSODRAFT_259959-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_259959-t26_1-p1
CAZy Family AA17
CAZyme Description polygalacturonase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
328 33977.97 7.2371
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 28 328 4.4e-63 0.8646153846153846

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 7.23e-65 25 328 10 321
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.
227721 Pgu1 8.38e-15 56 299 195 449
Polygalacturonase [Carbohydrate transport and metabolism].
215540 PLN03010 1.81e-14 54 328 122 386
polygalacturonase
178580 PLN03003 2.68e-14 26 295 61 337
Probable polygalacturonase At3g15720
215120 PLN02188 6.51e-12 66 289 122 348
polygalacturonase/glycoside hydrolase family protein

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.93e-192 25 328 60 363
2.68e-189 25 328 60 363
1.20e-182 25 328 57 360
3.92e-172 25 328 58 361
8.25e-171 25 328 55 358

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.55e-74 26 328 36 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
2.55e-74 26 328 36 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
6.39e-73 26 328 28 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
8.79e-71 26 324 28 333
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]
2.51e-66 26 328 28 336
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
3.72e-72 26 328 57 364
Endopolygalacturonase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=pgaB PE=1 SV=2
1.43e-70 26 328 63 371
Polygalacturonase OS=Penicillium janthinellum OX=5079 PE=3 SV=1
3.27e-70 26 328 67 376
Polygalacturonase OS=Penicillium griseoroseum OX=84562 GN=PGG1 PE=3 SV=1
1.04e-69 26 328 60 368
Probable endopolygalacturonase I OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pgaI PE=3 SV=1
1.42e-69 26 328 59 367
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000425 0.999548 CS pos: 19-20. Pr: 0.9515

TMHMM  Annotations      help

There is no transmembrane helices in PHYSODRAFT_259959-t26_1-p1.