CAZyme Information: ATEG_07623-t26_1-p1

Basic Information

• Species: Aspergillus terreus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
• CAZyme ID: ATEG_07623-t26_1-p1
• CAZy Family: GH55|GH55
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
507	CH476604|CGC8	55672.50	4.5299

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AterreusNIH2624	10551	341663	150	10401

• Gene Location: location=CH476604:560622-562356(-)

Full Sequence      

MRLRPTAAATLLALAPEHVLADRSVLPRGSSHQCCASLSSSEVGDKVIYPGDAAYETSVH
SYWAVNVQLEPACIVQPHSADDVAAVVQILTSAGGDSPCKFAVRSGGHMTWAGSNNIETG
VTIDLQMMNSTIYNEEAKVASILPGARWESVYKTLEEYNVVVPGGRTGPVGVGGFLLGGG
NSFHAARVGLACDNIINYEVVLASGRIVNANIESNTDLFKALKGGGNNFGIVTKYEVKAI
DNANLWGGISIYDNSTTDQQIDALVKFIDNIENDPYASWIGLWQYNSTTDKTLISSPLDY
TKPVAYPETFNDFYKIPNISSSTRFATLYNLTSELQQAAGYRDVFLTSTYLNSAKVLQKT
IDILNEKILKAKPVAQGKDWSIMVIIQPWPKIFWQRTQSNGVGNVLGLDRFDDNMLQVLY
DYSWDSEADDALFQCLCEEAMAELDDYAKSIGKYNEYIYLNYADKTQNPLRGYGDENVEY
IRAVAQRYDPDGVFQTQVPGGFKVSQA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	62	256	3.7e-55	0.4170305676855895

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.50e-18	67	494	28	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	6.67e-17	71	211	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	1.73e-05	67	234	61	233	cytokinin dehydrogenase
178402	PLN02805	5.72e-05	56	234	124	299	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANH22765.1|AA7	3.08e-19	63	294	112	339
CAI94231.1|AA7|1.1.3.-	2.91e-18	9	286	4	268
QRW22693.1|AA7	3.16e-18	26	495	16	477
QRD93627.1|AA7	5.39e-18	27	238	5	212
UDD63515.1|AA7	5.39e-18	27	238	5	212

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.07e-23	46	236	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]
6FYF_A	1.94e-23	46	236	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	1.94e-23	46	236	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	2.61e-23	46	236	21	205	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	3.50e-23	46	236	21	205	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	1.24e-178	31	507	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	4.25e-138	33	506	43	515	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	9.24e-85	29	505	28	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	1.30e-67	30	506	40	526	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|A0A023I4D6|PRX3_PENRO	2.65e-66	35	504	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000629	0.999323	CS pos: 21-22. Pr: 0.9730

TMHMM  Annotations     

There is no transmembrane helices in ATEG_07623-t26_1-p1.