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CAZyme Information: H310_04542-t26_1-p1

You are here: Home > Sequence: H310_04542-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 Aphanomyces invadans
Lineage Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
CAZyme ID H310_04542-t26_1-p1
CAZy Family GH47
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
550 KI913958|CGC2 59750.57 7.3217
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AinvadansNJM9701 15416 N/A 168 15248
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in H310_04542-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 136 499 1e-89 0.9912790697674418

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
225344 BglC 8.53e-06 125 410 32 290
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.70e-122 4 548 19 541
2.30e-108 4 547 15 535
2.50e-77 6 547 5 517
2.50e-77 6 547 5 517
1.74e-76 4 547 112 627

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.47e-26 118 500 6 350
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]
8.22e-26 118 500 6 350
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]
1.18e-25 118 500 39 383
Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_B Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_C Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
2.15e-25 118 500 39 383
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]
3.89e-25 118 500 39 383
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.02e-17 120 500 39 356
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
3.31e-14 119 500 44 387
Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
4.83e-14 120 500 26 343
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
3.03e-08 137 466 644 946
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999969 0.000035

TMHMM  Annotations      download full data without filtering help

Start End
38 60