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CAZyme Information: QRD06196.1

You are here: Home > Sequence: QRD06196.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRD06196.1
CAZy Family GT2
CAZyme Description Endo-polygalacturonase [Source:UniProtKB/TrEMBL;Acc:A0A7U2NPZ8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
365 36965.41 8.2894
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.15:80

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH28 40 365 3.3e-73 0.9661538461538461

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 1.20e-137 45 365 1 321
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.
177865 PLN02218 7.75e-29 82 359 143 420
polygalacturonase ADPG
227721 Pgu1 4.07e-26 87 292 189 408
Polygalacturonase [Carbohydrate transport and metabolism].
215426 PLN02793 1.68e-25 95 324 143 371
Probable polygalacturonase
178580 PLN03003 4.53e-23 29 297 35 304
Probable polygalacturonase At3g15720

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.05e-232 1 365 1 365
3.49e-169 1 365 1 364
1.42e-158 8 362 3 357
1.42e-158 8 362 3 357
4.50e-158 4 365 1 365

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.94e-156 28 362 1 334
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]
7.63e-143 20 365 1 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
3.09e-142 20 365 1 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
4.16e-138 28 365 1 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
9.26e-125 30 365 3 336
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
6.21e-170 1 365 1 364
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
1.21e-146 6 365 6 367
Polygalacturonase OS=Penicillium digitatum OX=36651 GN=PG1 PE=3 SV=1
2.38e-141 24 365 33 376
Polygalacturonase OS=Penicillium griseoroseum OX=84562 GN=PGG1 PE=3 SV=1
5.02e-140 14 362 9 358
Endopolygalacturonase 1 OS=Colletotrichum lindemuthianum OX=290576 GN=PG1 PE=3 SV=1
3.66e-139 30 365 36 370
Polygalacturonase 1 OS=Penicillium olsonii OX=99116 GN=PG1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000258 0.999746 CS pos: 27-28. Pr: 0.9233

TMHMM  Annotations      help

There is no transmembrane helices in QRD06196.1.