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CAZyme Information: EPrPVT00000024871-p1

You are here: Home > Sequence: EPrPVT00000024871-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 Phytopythium vexans
Lineage Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
CAZyme ID EPrPVT00000024871-p1
CAZy Family PL1
CAZyme Description Endopolygalacturonase 8
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
199 20566.06 7.7083
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PvexansDAOMBR484 11991 1223560 34 11957
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 43 199 3.2e-30 0.49846153846153846

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 6.70e-34 46 199 1 161
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 9.08e-10 96 199 199 310
Polygalacturonase [Carbohydrate transport and metabolism].
178580 PLN03003 8.70e-07 46 199 51 211
Probable polygalacturonase At3g15720
215540 PLN03010 5.06e-05 98 199 141 230
polygalacturonase
215426 PLN02793 1.14e-04 45 199 79 250
Probable polygalacturonase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.74e-87 10 199 11 201
2.54e-87 9 199 10 201
2.61e-87 23 199 26 202
3.95e-87 16 199 129 312
3.95e-87 16 199 129 312

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.71e-36 29 199 1 177
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]
4.18e-35 44 199 20 181
Polygalacturonase From Aspergillus Aculeatus [Aspergillus aculeatus],1IB4_A Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5 [Aspergillus aculeatus],1IB4_B Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5 [Aspergillus aculeatus]
5.53e-35 31 199 3 176
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]
1.42e-32 26 199 6 184
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.42e-32 26 199 6 184
Chain A, endo-polygalacturonase [Evansstolkia leycettana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.48e-40 18 199 18 204
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
7.03e-40 4 199 8 208
Probable endopolygalacturonase I OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pgaI PE=3 SV=1
1.91e-39 4 199 7 207
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2
1.91e-39 4 199 7 207
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
1.91e-39 4 199 7 207
Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000190 0.999796 CS pos: 19-20. Pr: 0.9519

TMHMM  Annotations      help

There is no transmembrane helices in EPrPVT00000024871-p1.