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CAZyme Information: PYU1_T009505-p1

You are here: Home > Sequence: PYU1_T009505-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 Globisporangium ultimum
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
CAZyme ID PYU1_T009505-p1
CAZy Family GT2
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
201 20443.45 10.0721
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GultimumDAOMBR144 15430 431595 140 15290
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 47 200 5.8e-22 0.4338461538461538

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 5.02e-19 73 200 191 321
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 7.25e-12 51 160 275 382
polygalacturonase ADPG
215426 PLN02793 1.28e-08 54 160 263 368
Probable polygalacturonase
227721 Pgu1 4.94e-05 75 122 352 399
Polygalacturonase [Carbohydrate transport and metabolism].
165802 PLN02155 1.18e-04 51 200 228 375
polygalacturonase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.04e-64 13 200 10 272
3.12e-63 76 200 3 127
2.74e-59 46 200 316 472
2.74e-59 46 200 316 472
2.74e-59 46 200 316 472

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.60e-19 73 197 207 334
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]
3.03e-18 73 200 214 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
3.03e-18 73 200 214 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
6.92e-17 73 200 206 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
8.80e-16 73 200 206 336
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
3.00e-20 46 200 208 364
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
1.47e-19 73 200 230 360
Probable endopolygalacturonase B OS=Aspergillus kawachii OX=1069201 GN=pgaB PE=3 SV=1
1.47e-19 73 200 230 360
Endopolygalacturonase B OS=Aspergillus niger OX=5061 GN=pgaB PE=1 SV=1
1.47e-19 73 200 230 360
Probable endopolygalacturonase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pgaB PE=3 SV=1
1.54e-19 76 200 240 367
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
0.000218 0.999787 CS pos: 27-28. Pr: 0.4487

TMHMM  Annotations      help

There is no transmembrane helices in PYU1_T009505-p1.