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CAZyme Information: RQM18777.1

You are here: Home > Sequence: RQM18777.1

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 Peronospora effusa
Lineage Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
CAZyme ID RQM18777.1
CAZy Family GT71
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
480 51143.64 6.5713
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PeffusaR13 8603 N/A 0 8603
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.15:10 3.2.1.15:10

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH28 47 352 3.6e-58 0.9261538461538461

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 1.75e-65 49 349 1 304
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 1.48e-21 46 334 106 448
Polygalacturonase [Carbohydrate transport and metabolism].
215540 PLN03010 1.54e-20 87 334 122 357
polygalacturonase
395231 Glyco_hydro_28 5.84e-18 354 466 52 170
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.
215120 PLN02188 3.40e-17 38 324 77 347
polygalacturonase/glycoside hydrolase family protein

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.21e-242 1 404 1 366
5.21e-174 104 354 1 251
3.31e-169 7 354 6 350
6.25e-167 1 367 1 354
9.93e-164 1 369 1 357

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.24e-58 33 354 10 332
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
7.24e-58 33 354 10 332
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
2.25e-57 33 354 2 324
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.71e-56 34 354 3 324
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]
2.75e-55 33 369 2 337
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.17e-68 6 354 7 356
Probable endopolygalacturonase I OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pgaI PE=3 SV=1
2.25e-68 1 354 1 355
Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1
2.25e-68 1 354 1 355
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2
2.25e-68 1 354 1 355
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
4.24e-62 32 369 25 359
Polygalacturonase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PGU1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000212 0.999783 CS pos: 20-21. Pr: 0.9773

TMHMM  Annotations      help

There is no transmembrane helices in RQM18777.1.