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CAZyme Information: KFA56039.1

You are here: Home > Sequence: KFA56039.1

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 Stachybotrys chartarum
Lineage Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
CAZyme ID KFA56039.1
CAZy Family GT32
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
631 KL650235|CGC12 67414.74 6.9306
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SchartarumIBT40293 11453 1280524 0 11453
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 83 629 5.7e-214 0.9047619047619048

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
199882 E_set_GO_C 4.87e-26 530 629 1 103
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 1.93e-23 545 629 5 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 5.79e-11 223 309 10 93
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 2.44e-10 257 468 1 136
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 4.70e-10 223 309 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.35e-289 17 631 98 711
2.44e-283 34 631 292 895
7.90e-274 42 631 119 710
2.25e-273 42 631 119 710
2.25e-273 42 631 119 710

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.82e-291 17 631 78 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
5.18e-291 17 631 78 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
1.04e-290 17 631 78 691
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
1.52e-142 139 629 177 659
Chain A, GALACTOSE OXIDASE [Fusarium graminearum]
3.12e-142 139 629 155 637
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
7.67e-141 139 629 196 678
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
3.04e-140 139 629 196 678
Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
4.19e-10 212 630 94 522
Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
1.92e-09 410 630 386 615
Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
8.74e-06 223 300 777 854
Kelch-like protein 29 OS=Mus musculus OX=10090 GN=Klhl29 PE=2 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000334 0.999674 CS pos: 22-23. Pr: 0.9748

TMHMM  Annotations      download full data without filtering help

Start End
7 29