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CAZyme Information: FOIG_04663-t36_1-p1

You are here: Home > Sequence: FOIG_04663-t36_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 Fusarium odoratissimum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
CAZyme ID FOIG_04663-t36_1-p1
CAZy Family CBM67|GH78
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
710 JH658277.1|CGC6 77022.95 9.7350
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006 16975 1089451 341 16634
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.9:34 1.1.3.13:3 1.1.3.-:1 1.1.3.7:1 1.1.3.47:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA5 154 708 2e-231 0.9149659863945578

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
199882 E_set_GO_C 5.86e-28 610 708 4 103
C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
401164 DUF1929 6.46e-27 618 708 1 91
Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase.
276965 Kelch 1.26e-12 300 387 10 94
Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965 Kelch 5.38e-12 300 386 57 140
Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965 Kelch 1.22e-09 334 546 1 137
Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 710 1 710
0.0 1 710 1 710
0.0 1 710 1 710
0.0 1 710 1 710
0.0 1 710 1 710

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 21 710 3 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
0.0 21 710 3 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
0.0 21 710 3 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
8.65e-149 200 708 137 637
Chain A, Galactose oxidase [Fusarium graminearum]
1.22e-148 200 708 137 637
Chain A, Galactose oxidase [Fusarium graminearum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.09e-147 200 708 178 678
Galactose oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GAOA PE=3 SV=1
2.18e-147 200 708 178 678
Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
7.84e-17 270 708 78 521
Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
1.32e-12 334 708 225 614
Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
1.42e-10 492 708 374 593
Putative aldehyde oxidase Art an 7 OS=Artemisia annua OX=35608 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000231 0.999746 CS pos: 20-21. Pr: 0.9776

TMHMM  Annotations      help

There is no transmembrane helices in FOIG_04663-t36_1-p1.