dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: THC92379.1

You are here: Home > Sequence: THC92379.1

Basic Information help

Species

Aspergillus tanneri

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri

CAZyme ID

THC92379.1

CAZy Family

GH16

CAZyme Description

Beta-mannosidase [Source:UniProtKB/TrEMBL;Acc:A0A4S3JB64]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
609		66966.12	5.0815

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtanneriNIH1004	13590	N/A	33	13557

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	18	567	2.2e-231	0.9166666666666666

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
199882	E_set_GO_C	1.99e-28	468	567	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	1.53e-23	490	567	14	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	1.56e-13	167	253	11	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	2.99e-13	167	253	58	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.
400133	Kelch_2	3.33e-06	202	244	3	45	Kelch motif. The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Drosophila kel is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.29e-275	1	567	119	686
9.22e-273	1	609	116	721
3.03e-271	1	605	116	718
1.78e-260	1	605	116	718
4.93e-257	1	606	116	710

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.76e-235	1	568	70	638	Glactose oxidase C383S mutant identified by directed evolution [Fusarium sp.]
1.01e-234	1	568	70	638	NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOG_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOH_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],2EIE_A Chain A, Galactose oxidase [Fusarium graminearum],2JKX_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ1_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ3_A Chain A, Galactose Oxidase [Fusarium graminearum]
3.93e-234	1	577	71	648	Chain A, Galactose oxidase [Fusarium graminearum]
3.31e-233	1	568	70	638	Chain A, Galactose oxidase [Fusarium graminearum]
5.96e-233	1	568	87	655	Crystal Structure of the Precursor of Galactose Oxidase [Fusarium sp.]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.14e-233	1	568	111	679	Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
4.29e-233	1	568	111	679	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
7.89e-12	365	567	303	521	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
2.83e-08	155	567	147	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000065	0.000000

TMHMM Annotations help

There is no transmembrane helices in THC92379.1.