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CAZyme Information: PPTG_13804-t26_1-p1

You are here: Home > Sequence: PPTG_13804-t26_1-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 Phytophthora parasitica
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
CAZyme ID PPTG_13804-t26_1-p1
CAZy Family GH78
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
512 KI669597|CGC2 51962.08 3.7926
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PparasiticaINRA-310 23240 761204 119 23121
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 197 505 7.9e-63 0.9384615384615385

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 2.66e-75 207 512 8 321
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.
178580 PLN03003 6.48e-23 252 479 115 337
Probable polygalacturonase At3g15720
215540 PLN03010 7.04e-23 252 482 141 357
polygalacturonase
215120 PLN02188 1.02e-22 250 473 122 348
polygalacturonase/glycoside hydrolase family protein
227721 Pgu1 7.86e-22 222 440 174 404
Polygalacturonase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.12e-297 1 512 1 512
2.86e-179 183 512 194 523
4.24e-178 183 512 32 361
1.19e-177 183 512 141 459
4.84e-174 183 512 10 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.35e-74 183 512 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]
2.22e-71 183 512 9 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
2.22e-71 183 512 9 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
4.87e-71 183 512 1 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
2.92e-70 183 511 1 336
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
9.01e-78 198 512 62 380
Endo-polygalacturonase OS=Sclerotinia sclerotiorum OX=5180 GN=PG1 PE=3 SV=1
2.41e-77 183 512 32 367
Endopolygalacturonase B OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaB PE=2 SV=2
2.41e-77 183 512 32 367
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
2.41e-77 183 512 32 367
Endopolygalacturonase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaI PE=1 SV=1
2.72e-76 183 512 33 368
Probable endopolygalacturonase I OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pgaI PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000242 0.999725 CS pos: 19-20. Pr: 0.9670

TMHMM  Annotations      help

There is no transmembrane helices in PPTG_13804-t26_1-p1.