CAZyme Information: ASPVEDRAFT_57496-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_57496-t33_1-p1
• CAZy Family: GH72|CBM43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
506		54878.17	5.0770

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=KV878139:630746-632355(-)

Full Sequence      

MALTATVLTALSSPVAATLPWAGTGYPPCDALIAAGLGDRVVLPTNTSYEPRIQSYWALN
PRRHPYCLVQPHSTQEVSTALTALLDGDASDPVSSGGDWHIAVRAGGHNLGDSNNIENGV
TIDLKYLNGTSYNAKTNIASIGPGAKWQDVYASLHKYGVVATGGRDGDVGVGGFLLGGGS
TYYMAKEGFGCDAIANFEVALANGTIVNANKNENADLWRALKGGGSNFGVVTRYDMEALP
DTKLARGQRSISTKYTGQFVDAIVDFTDKQQQHDDDALIAILAHVEGEDILATIEVNIQG
EQNSTGFDKFRKIPQTKPFEQNVGHLYEAARNSTLPGDAWALQTTLTFKNDAKMLNYAAS
AHSRFAADVQESIGKKSFYSIIFFQPLPSFFADISEKRGGNMFAETLRDGDAVLWTAGIF
VYTNQSDFAVASARMHEMVAELEQYSESIGADNQLRYLNYADFSQDPLGSYGEESVEHMH
RVAKKYDPESKFQTRIPGGFKISRVQ

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	54	493	1.3e-46	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.03e-13	65	210	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	1.07e-12	43	492	9	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	2.28e-15	27	240	8	215
UDD63515.1|AA7	2.28e-15	27	240	8	215
UJO23499.1|AA7	4.23e-15	38	240	36	230
QMW46638.1|AA7	7.17e-15	27	240	8	215
EGX49222.1|AA7|CBM1	1.73e-14	101	240	190	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	4.17e-16	27	237	8	207	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]
6FYG_A	7.39e-16	27	237	8	207	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]
6FYF_A	7.39e-16	27	237	8	207	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]
3W8W_A	7.51e-16	23	237	4	211	The crystal structure of EncM [Streptomyces maritimus],3W8W_B The crystal structure of EncM [Streptomyces maritimus],3W8X_A The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8X_B The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8Z_A The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus],3W8Z_B The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus]
6FYB_A	1.31e-15	27	237	8	207	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|A0A0U5GQ05|DRTC_ASPCI	5.07e-81	29	505	45	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	5.35e-69	29	505	8	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|M2T7Z1|TPCD_COCH5	2.06e-57	37	503	50	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A2P1DP98|MACF_PENTR	8.30e-42	5	493	21	506	FAD-dependent monooxygenase macF OS=Penicillium terrestre OX=374132 GN=macF PE=3 SV=1
sp|G3Y424|YANF_ASPNA	1.39e-41	12	493	97	567	FAD-dependent monooxygenase yanF OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=yanF PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.409034	0.590956	CS pos: 17-18. Pr: 0.5035

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_57496-t33_1-p1.