CAZyme Information: KFA49257.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA49257.1
• CAZy Family: CE3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
646		69565.39	4.3875

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: location=KL651513:3685-5625(-)

Full Sequence      

MVQLLAPAAVLAAAAFTPAYSRVIAHTNVVRDDTTVVGSRIPFIVRCPEGEAVLSAGDGI
RSDYLGCPGAVYEGADSAITRNVASPGDCAEICAENAACDKAVWDSVSLTCAVKAQEPEQ
TLFWVMRDGDRYTSITRNIIRDPSVEGEWTDLFRYPVVPIAAYVVPASPQPERILFFSAY
HNDTFGGTEGKTQFADFNFVTGEISHREVANTHHDMFCPGISQLEDGRIIINGGSNADAV
TFYEPFTNTFVEGPKMVQERGYQSSATTSTGKVFVLGGSFYGPLGGKNGELYDPATNEWT
DLPGADVNPILTDDFDGIWRSDNHAWLFAWKNESVFQAGPSKDQHWFQTNGTGAVSFSST
RDEDHAMCGVFVLYDAVKGKIFSAGGSPSYTSSPAQAHAHITTIGEPGVPAVVERIPDMA
FARSFANVVVLPDGTLLVTGGQRYAVVFTNDEANYLPELYNPETNEWTQLAPAGIPRNYH
SVSLLLPDASVLSAGGGGCATYGPDSPIIIDCGDQEYSHPDGQIFYPPYLFNEDGSRAER
PVITSVHSTRVEAGSTIRFTVSGGATTFSLIRMGTATHSVNTDQRRIPLYDAIIDGENVS
AVLPNDYGILLPGYYYLFAVSEAGVPSIAETIHVVFERCSNSTATA

Enzyme Prediction     

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

Family	Start	End	Evalue	family coverage
AA5	85	634	1.1e-205	0.9030612244897959

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
199882	E_set_GO_C	9.48e-28	535	634	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	9.04e-23	546	634	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	4.57e-09	414	485	39	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	2.20e-08	262	472	2	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.
276965	Kelch	1.68e-07	423	485	1	56	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EFQ27661.1|AA5_2|1.1.3.7|1.1.3.47	1.19e-242	61	635	139	710
UQC89470.1|AA5_2	3.97e-237	43	635	302	894
QGI83803.1|AA5_2	1.17e-224	43	634	121	708
QKD57968.1|AA5_2	2.35e-224	43	634	121	708
QGI66562.1|AA5_2	2.35e-224	43	634	121	708

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RYW_A	1.60e-244	61	635	119	690	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
6RYV_A	4.55e-244	61	635	119	690	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
6RYX_A	9.14e-244	61	635	119	690	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2EIC_A	1.79e-142	128	634	133	637	Chain A, Galactose oxidase [Fusarium graminearum]
1GOF_A	1.00e-141	128	634	133	637	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1S2N3|GAOA_GIBZE	4.40e-141	128	634	174	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
sp|P0CS93|GAOA_GIBZA	1.74e-140	128	634	174	678	Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
sp|Q9FYG4|GLOX1_ARATH	5.63e-15	215	635	176	615	Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
sp|A0A2H4HHY6|GLOX_ARTAN	4.01e-11	418	634	374	593	Putative aldehyde oxidase Art an 7 OS=Artemisia annua OX=35608 PE=1 SV=1
sp|Q3HRQ2|GLOX_VITPS	1.43e-10	410	635	294	522	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.041501	0.958467	CS pos: 21-22. Pr: 0.8270

TMHMM  Annotations     

There is no transmembrane helices in KFA49257.1.