CAZyme Information: ASPGLDRAFT_176772-t33_1-p1

Basic Information

• Species: Aspergillus glaucus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus
• CAZyme ID: ASPGLDRAFT_176772-t33_1-p1
• CAZy Family: GH15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
502		55030.37	5.6839

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AglaucusCBS516.65	11429	1160497	175	11254

• Gene Location: location=KV878905:480397-482115(+)

Full Sequence      

MKFCPSITALLFSIPLQADSGVGAADSCCAALSASSAGHQVVYPNQEPFVESVESYWSSS
VRLSPACIIQPESVEDVSVAVSTLVQEGGSLSSCKFAVRSGGHTVWTGAANIEDGVTIDL
SKMNSTTHHHENKTASIYPGARWGSVYKTLEKDNVTVAGGRGGPVGVGGFLLGGGNSFHS
ARVGFACDNVVNYQVVLASGAIIDANSNTNPDLFKALKGGTINFGIVTRFDMKTIPSEGI
WGGVVTYDWSTAYEQIPAFVNFTDNIHKDPYASLITMWQYDSKTDTNSVTNAMHYTKPVA
YPAAYDEFKQFANTSDGTRIDSQYTLVTELSQEGDSRNVFVTGTHVNNAQVIHKAAELHK
QVIEEAKKHAKSKSWNIVTMIQPWSKLFTERGSGMGGNVLGLERFDEDLIQTLYDYWWDD
KADDELFHRLARSIHQQLDGYAKMINADNEYVYLNYADKTQDPLKGYGEENVKYIRRVAE
KYDPHGVFQHQVPGGFKVSNVN

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	55	491	2.9e-59	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	6.48e-19	65	488	32	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.42e-14	65	206	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.
215242	PLN02441	0.001	61	229	61	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO16207.1|AA7	2.32e-20	48	497	109	556
ANF89368.1|AA7	1.77e-19	64	490	60	488
AEO58513.1|AA7|1.1.3.-	1.77e-19	64	490	60	488
QRW22693.1|AA7	4.01e-19	32	489	28	477
CDR44461.1|AA7	3.52e-18	64	261	69	269

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	3.59e-22	30	333	12	335	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]
6FYF_A	6.48e-22	30	333	12	335	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	6.48e-22	30	333	12	335	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	8.70e-22	30	333	12	335	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	1.17e-21	30	333	12	335	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|C8VPE5|SDCF_EMENI	5.26e-156	28	501	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|A0A0U5GQ05|DRTC_ASPCI	1.97e-140	21	501	37	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	9.14e-79	56	499	69	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A023I4D6|PRX3_PENRO	5.00e-64	42	500	44	509	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	5.00e-64	42	500	44	509	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
0.000719	0.999282	CS pos: 18-19. Pr: 0.9736

TMHMM  Annotations     

There is no transmembrane helices in ASPGLDRAFT_176772-t33_1-p1.