CAZyme Information: ASPGLDRAFT_63847-t33_1-p1

Basic Information

• Species: Aspergillus glaucus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus
• CAZyme ID: ASPGLDRAFT_63847-t33_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601	KV878890|CGC2	67054.94	6.4030

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=KV878890:513766-515620(-)

Full Sequence      

MKQYGKLALLAFLCLVQWVSGGHGFETDDVRTVRFGLDLTWEDYDGAGFTRKAILSNGQL
PAPTLRLRQGDNVEFVVKNQMPFSTTVHFHGIEQKGTPWSDGVPGLSQLPIEPGGQFIYR
WKATQYGSYFYHAHRRGQMDDGLYGAIHILADDSVERPFDKITKDPVELLQMRESEKSSQ
PILFSDWRRLTSEETYRTEQATGLDGFCTNTILINGKGSQYCLPRKRLNALTSAAQKMLL
GNNNVTDTGCMPPIEILEGHFWRNISAMPKSFYSGCQPTQGPTEIIKVNPAARWVSFDLM
TSAGVSTPTASIDEHSMYVYAIDGRYIEPMEVNGITISNGGRYSVFVKLDQPAGDYTIRA
PNTGINQIINTTATLSYDTLLKTQTRPSKPWVNEVGSNTTASTILFDETKVIPFPILTPA
LSVDNTYKLTVDHYNASYRWTLGNTSFSMSLEDATPLLFNTTSSPTDLTITTRNGSWVDL
IMVVKSPVQPPHPMHKHSNKFFVIGQGNGDFNYSSVAEAMRHIPENFNFKTPQIRDTFNT
PAAESEPTWLAIRYQVVNPGPFLLHCHLQVHLSGGMAIALLDGVDKWPVVPEGYRLPVLE
D

Enzyme Prediction     

No EC number prediction in ASPGLDRAFT_63847-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	49	577	2.2e-78	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	2.54e-86	424	583	1	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259919	CuRO_1_Abr2_like	1.76e-60	37	149	1	116	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259944	CuRO_2_Abr2_like	1.65e-58	180	377	1	137	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
274555	ascorbase	4.48e-56	57	591	26	532	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
177843	PLN02191	2.01e-55	57	592	48	556	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR86693.1|AA1	0.0	81	601	1	521
CAK37405.1|AA1	4.37e-263	3	596	5	599
BCR93194.1|AA1	1.77e-262	3	596	5	599
QMW25772.1|AA1	1.15e-254	7	599	8	585
QRD88217.1|AA1	1.15e-254	7	599	8	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	3.42e-38	26	582	19	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.46e-38	26	582	20	505	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	3.58e-38	48	582	83	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	8.69e-38	26	582	47	532	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	8.98e-38	48	582	83	542	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	2.71e-164	32	598	19	587	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	8.53e-153	33	594	40	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	1.58e-147	24	595	39	625	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|A0A1S7IUL2|MCE_TALPI	1.45e-142	11	594	8	592	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.04e-136	9	594	5	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000205	0.999767	CS pos: 21-22. Pr: 0.9863

TMHMM  Annotations     

There is no transmembrane helices in ASPGLDRAFT_63847-t33_1-p1.