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CAZyme Information: PYU1_T001030-p1

You are here: Home > Sequence: PYU1_T001030-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_T001030-p1
CAZy Family AA17
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
367 38404.18 8.4799
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 47 366 3.3e-60 0.9046153846153846

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 1.87e-73 48 366 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 1.26e-24 48 337 95 393
polygalacturonase ADPG
215540 PLN03010 1.00e-23 102 340 141 362
polygalacturonase
178580 PLN03003 3.93e-23 100 332 113 337
Probable polygalacturonase At3g15720
215426 PLN02793 2.31e-22 100 326 143 368
Probable polygalacturonase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.66e-144 29 366 150 480
1.81e-144 29 366 142 472
3.64e-144 29 366 142 472
3.64e-144 29 366 142 472
1.21e-143 10 366 11 363

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.92e-71 48 362 18 333
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]
2.41e-67 48 366 26 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
2.41e-67 48 366 26 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
5.97e-66 48 366 18 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.85e-64 29 366 1 336
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
2.66e-77 44 366 41 364
Polygalacturonase OS=Cochliobolus carbonum OX=5017 GN=PGN1 PE=3 SV=1
6.47e-76 13 366 14 367
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
6.47e-76 13 366 14 367
Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1
6.47e-76 13 366 14 367
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2
3.72e-74 31 366 39 376
Polygalacturonase OS=Penicillium griseoroseum OX=84562 GN=PGG1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000206 0.999797 CS pos: 19-20. Pr: 0.9809

TMHMM  Annotations      help

There is no transmembrane helices in PYU1_T001030-p1.