CAZyme Information: THC97792.1

Basic Information

• Species: Aspergillus tanneri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
• CAZyme ID: THC97792.1
• CAZy Family: GT1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
612	SOSA01000063|CGC1	67179.95	6.1363

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtanneriNIH1004	13590	N/A	33	13557

• Gene Location: location=SOSA01000063:37000-38955(+)

Full Sequence      

MNTLRYRLVWLTALLLSLAPWANANGQQVNATRNTVRYNLTLTWDDWAPAGTSRKMILTN
GQFPGPELRLQQGDDVEVLVVNNLPDPATIHFHGIEQINTPWSDGTPGLSQKNIAPGGRF
LYKWHAAQYGSYIYHAHSRGQMDDGLYGAIYIQPNDNVEKPFGQITDNKGEINAMHEAEK
KSAPVVLSDWRQLTSEEIWHAEEEMGRDAMCANALLVNGKGSVSCLSRQALDTATTPEQR
KVLGNTSFTDIGCLPPTNALAQGNFPHNLSAIPPSVFSGCTPSHGSTEKLLVDQAAQYVS
YDLISAAGISVITFSIDEHPMYVYAVDGRYVVPNLVDALTVPNGARYSVMVKLDKPAGDY
TVRVVNTGVNQILNTTAIMSYKTSQKTQQQPSTPCIDITGRPSTNCKVLDEGTIVPFPVE
VPAKEVAQTHVLNIDHYHASYLWTMGNSSYPLSLEESSPLLFDPSAAKTDLSIKTLNGTW
VDLVFHVVSSLQPPHPIHKHSNKFFVIGQGNGAWKYSSVAEAMKVIPESFNLKNPQIRDT
FVTPPAATGPTWLVIRYQVINPGAFFLHCHLQIHLSGGMGLALLDGVDHWPEIPVEYQGD
NAGFPPKELSSE

Enzyme Prediction     

No EC number prediction in THC97792.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	52	579	4.2e-79	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.22e-81	428	586	2	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.
259944	CuRO_2_Abr2_like	2.60e-60	183	382	1	138	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	1.65e-59	35	599	1	537	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.
259919	CuRO_1_Abr2_like	6.07e-58	38	153	1	117	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.
177843	PLN02191	4.67e-56	30	599	18	560	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR93194.1|AA1	1.53e-304	11	598	10	598
CAK37405.1|AA1	1.19e-301	11	598	10	598
QRD91048.1|AA1	5.01e-295	14	597	10	594
QMW31975.1|AA1	5.01e-295	14	597	10	594
QMW44009.1|AA1	5.81e-294	14	597	10	594

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.14e-46	47	596	15	534	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
3V9E_A	4.67e-41	23	585	55	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.18e-40	23	585	55	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]
5Z1X_A	6.62e-36	46	588	14	468	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
5LM8_A	8.88e-34	20	585	3	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	9.19e-171	22	593	6	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.98e-146	36	609	20	609	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	4.90e-145	36	609	25	612	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	5.56e-145	30	597	34	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	3.66e-140	40	606	28	601	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000355	0.999591	CS pos: 24-25. Pr: 0.9742

TMHMM  Annotations     

There is no transmembrane helices in THC97792.1.