CAZyme Information: ASPCADRAFT_506521-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_506521-t33_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
525		57341.93	5.0839

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907499:176060-177793(-)

Full Sequence      

MIAAALLLAVAVPVLAGPNTDAVSVCQHLHAVYPQYTVWDPTGTYATETFWNQSYYTNTV
KEYWNGVNANNRPACAFFPANAEQVSVAVQQLNKYPTAPFALKSGGHNFNAGFSSTNGGV
LLSFNENLSSTTRNPDGQTFDVGPGARWGDVYAVTEKTNQVVVGGRLANIGVAGYTLGGG
LSYYSAQYGLACDNVLNYEVVLANGTIVNANATSHPDLFWALRGGGNRYGIVTKFTIQGH
PLGTNGQIWGGMRFYNADKRQQIFEALSDFTRDYPDAKAAVIPTFDFGLPGALVSNPTLF
FFYDGANPPANAFVGLDKIESLFSTTKAQSYTELTNEAGGAKIYGINAAARVNTFPNMPP
AQMAQLLETHWTTYQSMIKNDSSRNLDIQIGTFTPQPLSVRIARASTERGGNALGLDPNN
GDRFWFENDLIWINPVCNDACPEYLRQVADTALEFFEKTLKGTKPTNWKSGNVDWVSVNP
LFMNDAADYQDVYASYGSANQARLENIAKTYDPNQFMFRQGGWSF

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	63	519	2.3e-56	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.57e-24	73	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.
223354	GlcD	7.34e-20	64	242	23	206	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	6.33e-08	73	234	65	233	cytokinin dehydrogenase
178402	PLN02805	8.29e-05	69	238	130	303	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7214923.1|AA7	1.87e-21	56	514	41	480
QRC92907.1|AA7	1.47e-20	54	271	46	262
UJO16207.1|AA7	1.54e-20	73	237	128	291
UNI23960.1|AA7	3.21e-19	73	241	48	216
UJO20529.1|AA7	3.36e-19	73	517	90	508

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	4.19e-22	42	276	15	242	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	7.53e-22	42	276	15	242	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	7.53e-22	42	276	15	242	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]
6EO5_A	1.12e-21	73	242	48	218	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	1.12e-21	73	242	48	218	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B1P2|A2372_ARTBC	4.19e-67	52	516	43	488	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	2.52e-57	60	514	68	500	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	2.86e-51	56	514	28	463	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	3.01e-48	63	513	69	503	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	5.98e-43	48	517	129	566	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
0.000212	0.999775	CS pos: 16-17. Pr: 0.9778

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_506521-t33_1-p1.