CAZyme Information: ASPSYDRAFT_212175-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_212175-t33_1-p1
• CAZy Family: GH154
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
505		54642.92	5.4418

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878597:178667-180288(+)

Full Sequence      

MALVATALTALTSLAAANPSWAGTGYPPCDALITAGLGNRVVLPSNASYEPRIQSYWALN
TRRHPYCLVQPHTTQEASTALAALLGTGPEISSGAGDWHIAIRAGGHNLGDSNNIANGVT
IDLQYLNSTSYNAKTNIASIGPGAKWEDVYASLHEYGVVATGGRDGDVGVGGFLLGGGST
YYMAKQGFGCDSIVNFEVVLANGTIVNANKDQNADLWRALKGGGSNFGLVTRYDMEALPD
RKLARGQRSMSAKYTGQFVDAVVDFTDKQQKYDDDALIAIVAHVEGEDILATIEVNIEGV
QNSTGFDKFRRIPQIKQFEQNVGYLYEAARNSTLPGDAWALQTTLTFKNDAKTLNYAASA
HSRFAADVEKSIGKKSFYSVSFFQPLPSFFADISERRGENMFAGTLRDGNAVLWTGGLFV
NTNQSDFAVASARMHELVAELEQYSESIGADNQLRYLNYADFSQDPLGSYPEESVEHMHK
VAAKYDPEGKFQTRIPGGFKISRVH

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	55	492	4.5e-47	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.76e-14	62	491	29	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.46e-12	65	209	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	1.71e-16	28	239	8	215
UDD63515.1|AA7	1.71e-16	28	239	8	215
QMW46638.1|AA7	5.39e-16	28	239	8	215
CAI94231.1|AA7|1.1.3.-	1.13e-15	30	243	17	232
CCA72155.1|AA7	2.88e-15	65	239	95	277

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.32e-17	27	236	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]
6FYF_A	2.34e-17	27	236	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]
6FYG_A	2.34e-17	27	236	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]
3W8W_A	2.39e-17	23	236	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	4.17e-17	27	236	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	6.92e-81	29	504	45	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	1.09e-67	29	504	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	5.61e-51	44	502	57	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|G3Y424|YANF_ASPNA	4.17e-43	12	503	104	578	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
sp|D4B1P2|A2372_ARTBC	1.15e-41	29	501	29	499	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000400	0.999566	CS pos: 22-23. Pr: 0.9607

TMHMM  Annotations     

There is no transmembrane helices in ASPSYDRAFT_212175-t33_1-p1.