CAZyme Information: ASPVEDRAFT_142668-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_142668-t33_1-p1
• CAZy Family: CE1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
602	KV878137|CGC1	66048.62	4.6891

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878137:805320-807230(+)

Full Sequence      

MAPLRTLVLLTTLASQAFALAVRRTTSVASVPESAWDSLNETISGHLRNGEPMLAPCYLR
YNGESQTPDLDQCAKLQQDGGDLSFATGQFGYYVQSQWGACQATGDSCTFGLIRPDILTP
VLDKCEQGSVPTKYVDVQSVEDVQRTLVFAGEHNLRLVVKNTGHDYMGRSSAPDALALWM
HNLQPPIELNKDFIADGCSESSGDSITFGAGQQFGGIYDFVEPLGYRIVGGSSITVGAAG
GWITGGGHSMLTNELGLGVDSVQQLKAVLPNGKHVTANRCQNQDIFFALRGGGGGTFGVI
TEMTTRVYPKKETQFVEMIFTNLLPVQQRRLMDILVGNAEKWAEEGWGGYITMLSVGTGV
FIATPLLTHEEAEQSMKPLAEFATTFNLGIVKVQSTENFREGLDPFVQIQKFGIFPGSAW
ALSSRIVKRESFTQDKQEELSDILSNFLNVQQNLLEPSLQILVLCLTMPAVYSKKSMPES
DLPGGPGHPSIAPHWREGIWQVLHFRTYDGSIDDPDLVQRIAQRAHDVMEPLRAFTPGSG
AYLNEADPWEPDHINSFWGEENYARLLKIKREVDPSNLLMVHQGVGWDEGDGRFACYPDV
TA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	137	315	4.9e-40	0.3624454148471616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	2.16e-18	131	278	1	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
223354	GlcD	6.43e-18	138	579	39	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	2.79e-10	541	586	1	45	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
273751	FAD_lactone_ox	2.35e-06	128	324	12	197	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	1.91e-38	125	591	592	1055
QKD57322.1|CBM91|GH43_11	1.91e-38	125	591	592	1055
UJO23499.1|AA7	6.47e-16	130	585	62	483
UJO20529.1|AA7	4.40e-12	130	600	89	530
CBX96933.1|AA7|CBM18	5.73e-12	141	586	223	643

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	2.56e-59	36	593	43	570	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	6.97e-50	34	589	43	586	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	1.28e-12	139	585	53	459	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYG_A	1.70e-12	139	585	53	459	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYB_A	2.25e-12	139	585	53	459	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A7L8UYL4|FFSJ_ASPFV	1.16e-78	36	593	26	593	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|G4MWA7|OXR2B_MAGO7	1.72e-76	28	596	20	576	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|P0CU32|CHEF_CHAGB	5.56e-72	36	596	69	608	FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1
sp|Q0V6Q5|PHMC_PHANO	3.06e-65	26	399	17	357	FAD-linked oxidoreductase phmC OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=phmC PE=3 SV=2
sp|D4B1Z7|A2478_ARTBC	3.02e-62	33	588	39	560	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000290	0.999698	CS pos: 19-20. Pr: 0.9719

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_142668-t33_1-p1.