dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: QRC92079.1

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Basic Information help

Species

Parastagonospora nodorum

Lineage

Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum

CAZyme ID

QRC92079.1

CAZy Family

AA7

CAZyme Description

Apple domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2ESB1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
711		76133.22	8.4140

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

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	161	709	4.2e-216	0.8962585034013606

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
199882	E_set_GO_C	1.43e-26	611	709	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	5.09e-26	619	709	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	1.39e-12	261	379	16	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	3.30e-09	336	546	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	3.64e-08	489	571	39	112	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
0.0	1	711	1	711
0.0	15	711	9	702
7.46e-297	11	711	5	707
1.15e-279	8	711	3	710
1.15e-279	8	711	3	710

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.02e-272	26	711	2	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
1.62e-271	26	711	2	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2.30e-271	26	711	2	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
1.78e-148	180	710	121	638	Chain A, Galactose oxidase [Fusarium graminearum]
2.46e-148	180	710	143	660	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
4.47e-147	180	710	162	679	Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
6.30e-147	180	710	162	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
3.22e-16	291	708	94	520	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
1.09e-13	483	709	381	614	Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
3.94e-09	479	709	370	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
0.107436	0.892527	CS pos: 27-28. Pr: 0.8500

TMHMM Annotations help

There is no transmembrane helices in QRC92079.1.