CAZyme Information: ASPVEDRAFT_148720-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_148720-t33_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
508	KV878127|CGC19	55067.67	4.6759

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=KV878127:435943-437684(-)

Full Sequence      

MRLAPTVAAALLGLVSELTLATGTDTSPQASADQCCAALSKSKVGDKVVRPNSAAYKKSV
QSYWSVNVQLEPTCIVQPQSADDVSAVVKTLTTAGGELPCKFAVRSGGHMTWAGSNNIET
GVTVDLSNMNSTVYDKEAGVASILPGARWQAVYKTLEEYNVVVPGGRTGPVGVGGFLLGG
GNSFHAARVGLACDSVENYEVVLASGRIVNANNSTNRDLFKALKGGANNFGIVTKYDLKT
IDNAHMWGGLTVFTPNSTEQVISSAVKFVDNIEKDPYASWIGLWTYNATTDELTDGSLMQ
YTKPVPRPAAYNDFYKIPNISSTNGPQTLLEATTAIQQAGGKRNAFLTGTYINSADILRK
ALEIQKNKIDDAKTLAKGKDFVLVVIIQPWPKLFWQRNAGNGIGNVLGLERFDENMIQVL
YDYTWEEEADDGVFQRLTEESLNELDEYARDSGKYNEYVYLNYADGSQNPLAGYGDESVE
YMRQVAQRYDSDGVFQTQVPGGFKVSEA

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	61	497	9.9e-58	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	6.62e-20	68	495	28	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	9.73e-16	72	212	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.
178402	PLN02805	1.53e-04	65	239	130	303	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	8.98e-04	68	235	61	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW22693.1|AA7	1.30e-19	30	290	19	278
CAI94231.1|AA7|1.1.3.-	4.82e-19	42	281	30	262
ANH22765.1|AA7	5.42e-17	64	240	112	286
ANF89368.1|AA7	1.06e-16	11	240	3	227
AEO58513.1|AA7|1.1.3.-	1.06e-16	11	240	3	227

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	4.07e-20	47	237	21	205	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
3RJ8_A	5.74e-20	42	281	8	240	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
6FYF_A	7.29e-20	47	237	21	205	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
6FYG_A	7.29e-20	47	237	21	205	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]
6FYE_A	9.75e-20	47	237	21	205	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	6.25e-164	32	508	5	479	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	1.33e-128	34	507	43	515	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	1.25e-76	39	506	45	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	6.84e-68	23	507	29	526	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	1.52e-64	10	505	6	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000373	0.999620	CS pos: 23-24. Pr: 0.5311

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_148720-t33_1-p1.