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CAZyme Information: EPrPRT00000016305-p1

You are here: Home > Sequence: EPrPRT00000016305-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 Pythium arrhenomanes
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
CAZyme ID EPrPRT00000016305-p1
CAZy Family GH16
CAZyme Description Polygalacturonase.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
294 ParrATCC12531_SC00339|CGC1 30891.39 7.5112
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531 13857 1223556 52 13805
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 8 289 5e-64 0.8123076923076923

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 2.75e-65 1 290 15 310
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.
215540 PLN03010 3.38e-23 39 269 141 357
polygalacturonase
178580 PLN03003 2.53e-20 39 266 115 337
Probable polygalacturonase At3g15720
215426 PLN02793 4.34e-20 39 260 145 368
Probable polygalacturonase
177865 PLN02218 1.83e-19 38 260 157 382
polygalacturonase ADPG

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.82e-144 2 294 174 466
1.82e-144 2 294 174 466
7.35e-144 2 294 174 466
1.92e-143 2 294 182 474
1.31e-142 2 294 93 385

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.03e-68 2 291 33 327
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]
1.03e-63 2 291 41 334
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.03e-63 2 291 41 334
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
2.59e-62 2 291 33 326
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.42e-58 1 283 32 318
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
1.34e-71 2 290 60 353
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
4.57e-67 1 291 63 357
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
4.57e-67 1 291 63 357
Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1
4.57e-67 1 291 63 357
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2
3.28e-66 2 293 72 373
Polygalacturonase OS=Penicillium griseoroseum OX=84562 GN=PGG1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000067 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in EPrPRT00000016305-p1.