CAZyme Information: SHO78428.1

Basic Information

• Species: Malassezia sympodialis
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia sympodialis
• CAZyme ID: SHO78428.1
• CAZy Family: GH55
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
902	LT671824|CGC10	98358.21	5.1103

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MsympodialisATCC42132	4618	1230383	143	4475

• Gene Location: location=LT671824:568404-571112(+)

Full Sequence      

MLILPYVAAIWAVLSCSGLVSADGGKAKNQYEVVVKDTLASAMMLGLANENTAFIFDKVE
GNFQKTMSGKPTWASLVDLNTFEVRGIDAQTNPFCAAGMTLGNGSYIVVGGNSAISYGGQ
GTNLPNGSVATGPVAPYQDFDGRRVVRIMEPNEDASQLNWVDQYNSPNQMDSPRWYPGIE
GLADGSVVIIGGATNGGFINRNTPNVDPAYATSSSNPTPGVWDQGGANPSYEFWPPTGKP
KPAISDFMVKTSGLNMYAHTYLMPSGKIFMQANYSTTLWDWSNDKYYDLPDMPGQITRVY
PASGATAMKPLTPKNNYTPTILFCGGFHMTDDEWGNFTAPNINVYDREGSTDCSSITPES
ASGDMDKNVQYVKEEDLPEPRSMGQFIQLPNGKMVIVNGASRGLAGYGNTTWNKVKDKGG
NTVYLEGMSQSPTLRPVVYDPEKPQGQRLEYDGFGHSDYPRLYHSSAILAPDGSVLVAGS
NPHMDVAILPPNDQLDTKYEAFNTTYVMERWYPEYYFEERPVPQNLPKVIGYGGDPFNIT
VPAKYMNPNNNANDMANNTRIFVIRPGFSTHAYNFGQRSLELENTFSVQNDGSVEFMVNP
MPTNMNLFVPGPALLFVTVNGVPSHGKLIMIGKQNPGLVPFNLKPGPEPKPLPKPQLNSK
YSKPAPQLGMSSKSGDDDDGLSGGAIAGIVIGILVALAIIAAILFFVWRHNRQKQTMAQY
STIGRPQAPASSGSFNQESATTNPRYGTSSAGWSQTDMSQQPMMMRNDSQMSFTDETLGP
AFSDVNHARSLDNQTPNGMAMNPEPSSQTVLHQNSNPFMQESYSDHNYTSPSSLAQTSQL
APPLTSSTVMAPAGSRQPYMVPQPTTHWNDIPTRPQMMGPREMPQSNLQQHITANQANQP
RY

Enzyme Prediction     

EC	1.2.3.15:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA5	26	640	1.6e-221	0.9680284191829485

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
401164	DUF1929	2.94e-22	527	631	3	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.
199882	E_set_GO_C	5.27e-21	515	631	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.
399910	Glyoxal_oxid_N	6.56e-21	76	326	50	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.
213052	TM_EGFR-like	6.14e-04	685	715	7	38	Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.
397323	Atrophin-1	0.005	736	900	139	303	Atrophin-1 family. Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SHO78428.1|AA5_1	0.0	1	902	1	902
AYO41394.1|AA5_1	0.0	12	893	2	865
AXA48404.1|AA5_1	0.0	10	893	9	874
SAM67814.1|AA5_1	7.48e-225	7	787	19	743
UOP57117.1|AA5_1	4.92e-224	21	734	34	729

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UNM_A	1.00e-08	138	631	229	614	Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans],4UNM_B Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans]
5LXZ_B	4.62e-07	138	631	218	603	W288A mutant of GlxA from Streptomyces lividans: Cu-bound form [Streptomyces lividans TK24]
5LQI_A	4.64e-07	138	631	223	608	W288A mutant of GlxA from Streptomyces lividans: apo form [Streptomyces lividans 1326],5LQI_B W288A mutant of GlxA from Streptomyces lividans: apo form [Streptomyces lividans 1326]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q01772|GLOX_PHACH	8.67e-60	47	636	44	554	Aldehyde oxidase GLOX OS=Phanerodontia chrysosporium OX=2822231 GN=GLX PE=1 SV=1
sp|Q3HRQ2|GLOX_VITPS	4.35e-36	76	631	78	521	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
sp|Q9FYG4|GLOX1_ARATH	1.75e-33	73	631	155	614	Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
sp|A0A2H4HHY6|GLOX_ARTAN	6.22e-32	78	631	133	593	Putative aldehyde oxidase Art an 7 OS=Artemisia annua OX=35608 PE=1 SV=1
sp|D4AUF1|WSCD1_ARTBC	2.92e-26	85	632	475	904	WSC domain-containing protein ARB_07867 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07867 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000637	0.999361	CS pos: 22-23. Pr: 0.5407

TMHMM  Annotations     

Start	End
686	708