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CAZyme Information: EKG17382.1

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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 Macrophomina phaseolina
Lineage Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
CAZyme ID EKG17382.1
CAZy Family GH43
CAZyme Description Glycoside hydrolase family 28
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
378 38198.97 4.1928
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MphaseolinaMS6 14712 1126212 906 13806
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 58 373 7.2e-72 0.9753846153846154

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 9.25e-128 62 378 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.
227721 Pgu1 3.20e-24 104 305 189 408
Polygalacturonase [Carbohydrate transport and metabolism].
215540 PLN03010 5.43e-23 100 377 122 393
polygalacturonase
177865 PLN02218 1.20e-21 114 374 158 422
polygalacturonase ADPG
178580 PLN03003 7.97e-18 113 367 114 364
Probable polygalacturonase At3g15720

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.60e-169 45 378 146 486
1.51e-165 47 378 111 449
2.57e-164 45 378 101 440
2.76e-164 34 376 22 368
4.04e-164 46 378 28 363

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.63e-164 46 376 2 335
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]
6.20e-155 40 378 5 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
3.57e-154 40 378 5 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
3.81e-154 46 378 2 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.37e-149 45 378 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
2.21e-158 38 378 37 380
Endo-polygalacturonase OS=Sclerotinia sclerotiorum OX=5180 GN=PG1 PE=3 SV=1
4.02e-157 46 378 30 363
Endopolygalacturonase A OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaA PE=2 SV=1
4.02e-157 46 378 30 363
Probable endopolygalacturonase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=pgaB PE=3 SV=1
3.28e-156 42 378 26 363
Endopolygalacturonase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaB PE=2 SV=2
1.33e-155 46 378 30 363
Probable endopolygalacturonase A OS=Aspergillus parasiticus OX=5067 GN=pgaA PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.063484 0.936485 CS pos: 31-32. Pr: 0.5191

TMHMM  Annotations      download full data without filtering help

Start End
7 26