CAZyme Information: AKAW_05468-t41_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: AKAW_05468-t41_1-p1
• CAZy Family: GH18
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
508	DF126459|CGC7	56816.92	6.6838

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

• Gene Location: location=DF126459:223011-224796(+)

Full Sequence      

MYNLDRFPGPTVEARSGDRLIVSVTNHLEEEPISIHWHGVHIENAMDGAVGVTQRPIPPG
STFTYNFTIPADQSGTFWYHAHSGLLRVDGLYGGLIVHKPSPKPTVRGLLARADQRELGS
YDKDILLLVGDWYHRSADQVYSWYMRAGSFGNEPVPDSLLINGVGHFDCSMAVPARPVDC
ILRQMNVSYLDAKGDATYRVRVVNTGSVAGVTLGFQNREFTLIQVDNIDVEQQDSNSAGV
LYPGQRMDIMLRPSPDETPSSLTIDLDKECFRYPNPALASIQTFDITNSPNNLSSSIYSS
NNTISLSEVATRKSLLSGLPAKAHQTHVVYTKIEKLSINHNVPYGFFNRTSWRPQIDTPL
IDIPREKWDKNQLVLSTGPTTSRRLSSDQDKDLWIDLVVNNLDDSGHPFHMHGHHFYILR
TYQAPVGWGAYNPFTDAHPPGLAPHPASSSRTDSPYDLSRAQLRDTVYIPSRGHAVLRFR
ADNPGIWLFHCHIIWHQASGMAMLLQIE

Enzyme Prediction     

No EC number prediction in AKAW_05468-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	6	502	9.1e-89	0.952513966480447

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
177843	PLN02191	6.19e-63	6	505	50	544	L-ascorbate oxidase
274555	ascorbase	7.18e-63	6	501	28	517	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.
259977	CuRO_3_MCO_like_4	9.58e-60	328	507	2	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
225043	SufI	5.07e-55	7	502	61	443	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
274556	laccase	4.04e-52	6	503	30	515	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS06095.1|AA1	0.0	46	508	1	460
BCR93452.1|AA1	0.0	46	508	1	460
CAK44017.1|AA1	7.33e-314	7	507	110	586
QMW37919.1|AA1	1.58e-229	7	507	120	598
QRD88142.1|AA1	2.86e-229	7	507	137	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.08e-50	6	505	30	477	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]
3V9E_A	3.04e-48	8	503	96	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	7.98e-48	8	503	96	538	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]
1AOZ_A	6.56e-46	6	504	30	520	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]
5LM8_A	6.16e-41	6	502	50	499	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|I1RMG9|FET3_GIBZE	4.03e-57	6	501	52	490	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|Q6CII3|FET3_KLULA	4.60e-56	7	505	56	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|P43561|FET5_YEAST	5.28e-54	7	502	49	508	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|K7NCS2|FETC_EPIFE	3.71e-53	6	502	50	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P78591|FET3_CANAX	2.58e-51	5	505	50	496	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999427	0.000607

TMHMM  Annotations     

There is no transmembrane helices in AKAW_05468-t41_1-p1.