CAZyme Information: THC94179.1

Basic Information

• Species: Aspergillus tanneri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
• CAZyme ID: THC94179.1
• CAZy Family: GH2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
537	SOSA01000222|CGC1	60850.69	6.8773

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=SOSA01000222:34427-36331(-)

Full Sequence      

MERQTSRRRKHLQVNEQSKTGQSRSDTRQKESAAKHEKHRSYRLLLYPLVVCFLIGLVFL
YQSSTPDPILSVLSRPRNHRQDASPRAHDPDAFRPRIELHPEDHVYRDPRTQHYDWVVTS
DLLRPDGVLKQVYLINGLLPGPTIEARSGDRLVVKVKNTLDIPISIHWHGIHISNSMDGV
PSVTQCAISPWSTFTYNFTLPSYQSGTFWYHAHSGVIRGDGLYGGLVVHEPVPKPTVRGL
MARDSADIQSSYDREFLFLIGDWYHQPAEEILAWFMSIASFGNEPVPDSLLVNGVGAFNC
SMAVPAQPVDCIQQELNLSYLDTDIEPGYKLRIVNTGSLAGFTLSFENHQICLIQVDSID
TKPQEPTSAAGILYPGQRMDVILLPKSHNNTQSSMTIHLDQECFNQPNPALTHIQAIPMS
SFHSNRQETPQTIERFIDLSQTPSSETILSHLPKKPHDTHVVYTKIQKLSINHNIPNGFF
NHTSWFPQRHPPIPLNALSREKWDNNQFYIVTGDNATWVDIVVNNLDEGGHPFHLVN

Enzyme Prediction     

No EC number prediction in THC94179.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	128	438	2.5e-70	0.7402234636871509

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259926	CuRO_1_Diphenol_Ox	2.49e-51	113	229	2	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats 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.
259869	CuRO_1_LCC_like	1.92e-49	112	229	1	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
274555	ascorbase	1.14e-47	111	357	1	241	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.
259927	CuRO_1_tcLCC2_insect_like	5.19e-45	126	229	1	105	The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. 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, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats 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	6.72e-44	114	473	26	388	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW37919.1|AA1	1.03e-225	25	535	4	510
QRD88142.1|AA1	1.50e-224	1	535	1	527
QMW25836.1|AA1	1.50e-224	1	535	1	527
CAK44017.1|AA1	3.54e-192	42	535	14	490
UPX44859.1|AA1	7.41e-177	92	535	73	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.60e-35	111	535	2	396	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
1AOZ_A	1.94e-35	112	432	4	314	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	4.69e-35	111	383	67	315	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.69e-35	111	383	67	315	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]
3FPX_A	4.26e-30	115	535	7	399	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	1.97e-44	109	535	59	484	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|K7NCS2|FETC_EPIFE	7.20e-44	111	535	22	416	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	4.87e-43	109	383	59	319	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	3.90e-41	109	535	59	484	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|E9R598|FETC_ASPFU	5.12e-41	111	535	22	416	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999972	0.000035

TMHMM  Annotations     

Start	End
44	61