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CAZyme Information: PPTG_03220-t26_1-p1

You are here: Home > Sequence: PPTG_03220-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_03220-t26_1-p1
CAZy Family AA3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
536 57654.71 4.1299
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

No EC number prediction in PPTG_03220-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 36 348 2e-82 0.9903225806451613

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
225344 BglC 1.52e-32 37 356 42 378
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098 Cellulase 4.49e-25 59 341 17 270
Cellulase (glycosyl hydrolase family 5).
411343 exchanger_TraA 0.001 387 485 305 391
outer membrane exchange protein TraA. TraA, together with its partner TraB, mediates a large scale exchange of outer membrane lipoproteins, and lipids, between closely related strains or clonally identical cells, certain delta-proteobacterial species such as Myxococcus xanthus. The exchange mechanism is likely to involve fusion of outer membrane, probably done to coordinate the social behaviors these bacteria display.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 9 528 8 521
2.95e-65 33 366 57 392
8.99e-65 33 371 64 404
1.20e-64 33 374 59 402
5.46e-64 33 382 63 414

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.31e-64 41 368 29 375
Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
8.46e-64 41 368 29 375
The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
4.84e-63 41 368 62 408
Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_B Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_C Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
4.84e-63 41 368 62 408
Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_B Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_C Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
6.77e-63 41 368 62 408
Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.61e-59 43 356 57 369
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
3.46e-53 33 356 55 379
Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
3.70e-47 1 368 10 368
Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2
2.33e-38 33 366 638 994
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
7.13e-34 42 366 62 441
Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.004422 0.995550 CS pos: 19-20. Pr: 0.5719

TMHMM  Annotations      download full data without filtering help

Start End
513 535