logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: K441DRAFT_675313-t45_1-p1

You are here: Home > Sequence: K441DRAFT_675313-t45_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 Cenococcum geophilum
Lineage Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
CAZyme ID K441DRAFT_675313-t45_1-p1
CAZy Family GH63
CAZyme Description copper radical oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
678 KV748185|CGC1 75541.09 5.5664
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Cgeophilum1.58 14745 794803 38 14707
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in K441DRAFT_675313-t45_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA5 151 676 1.9e-121 0.37236533957845436

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
199882 E_set_GO_C 4.11e-39 576 673 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 9.69e-29 587 673 2 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.
399910 Glyoxal_oxid_N 7.78e-10 210 442 2 243
Glyoxal oxidase N-terminus. This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.
276965 Kelch 7.17e-06 436 542 12 103
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 3.25e-04 267 331 10 66
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
7.25e-93 204 673 10 510
1.23e-54 208 676 48 505
2.08e-52 208 676 39 496
1.19e-49 209 674 140 594
2.22e-49 201 674 101 568

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.35e-36 255 671 270 687
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2.35e-36 255 671 270 687
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
4.22e-36 255 671 270 687
Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
9.96e-28 240 671 207 635
Glactose oxidase C383S mutant identified by directed evolution [Fusarium sp.]
1.83e-27 216 671 181 636
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
3.38e-35 195 671 15 519
Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
2.14e-32 222 676 460 906
WSC domain-containing protein ARB_07867 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07867 PE=1 SV=1
4.52e-30 254 673 174 614
Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
1.41e-26 240 671 248 676
Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
1.87e-26 240 671 248 676
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000036 0.000010

TMHMM  Annotations      help

There is no transmembrane helices in K441DRAFT_675313-t45_1-p1.