CAZyme Information: KAF7628570.1

Basic Information

• Species: Aspergillus flavus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus
• CAZyme ID: KAF7628570.1
• CAZy Family: GT1
• CAZyme Description: Laccase, putative [Source:UniProtKB/TrEMBL;Acc:B8MZ52]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
620	AAIH03000072|CGC24	69115.77	5.7657

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflavusNRRL3357	14313	332952	0	14313

• Gene Location: location=AAIH03000072:2983710-2985919(-)

Full Sequence      

MERKPSRRKSRIFETPERNESDTGSQNAPARRTTKYWPCGIVICPLILCILSALLFLQQF
TTPDPLRSVLSSTKVHHGETLHSQVHNPDLARPSIELHPEDHVYRGAVTQHLDWVVAEDY
LRPDGVLKQVYLVNGIFPGPTIEACSGDTLLINVTNALQGEPISIHWHGLHVHNTMDGVP
GVTQNAIPPGSTFMYNLTIPQDQSGTFWYHGHTGTSRADGLYGGFVVHAPSSRPTVRGLM
ARDSAESLQYGYEREFLLLIGDWYHQPGAQVLAWYMSIASFGNEPVPDSLLINGAGSFDC
SMAVPARPVDCIEQQANLSYLSDIDTSFRLRVVNTGSLAGFTLSFENKPLTLIQVDSTEV
EPQEAPSAGILYPGQRMDVILQPSKEDLTSLTIHLDRDCFNYPNIALTPTQTFPITPSHS
PSLPQSLPENNLDLQNTPSKPSLLSNIPENPTQTQVIYTKIQKLSINHNIPNGFFNRTSW
RPQPDTPLNTLPRDKWDDNQFSFAVPDSEWVDVVVNNLDEGGHPFHLHGHHFYILRVYEA
PIGWGSYNPFVDSGPPGLESESGYDLSRAMLRDTVYIPSRGYAVLRFRADNPGVWLFHCH
IVWHLASGMAMLVDVGEYNS

Enzyme Prediction     

No EC number prediction in KAF7628570.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	126	610	6.1e-92	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.08e-77	109	609	1	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.
177843	PLN02191	8.80e-72	102	612	17	543	L-ascorbate oxidase
225043	SufI	1.15e-65	124	618	48	451	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].
259977	CuRO_3_MCO_like_4	8.08e-62	456	615	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.
215324	PLN02604	1.15e-59	107	616	22	547	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD88142.1|AA1	0.0	1	620	1	620
QMW25836.1|AA1	0.0	1	620	1	620
QMW37919.1|AA1	0.0	18	620	1	603
UCK58312.1|AA1	0.0	176	620	1	445
CAK44017.1|AA1	2.03e-245	26	615	2	586

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.35e-59	109	613	2	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]
1AOZ_A	4.35e-57	110	616	4	524	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	1.43e-50	114	611	71	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.73e-50	114	611	71	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]
5EHF_A	4.32e-45	113	613	7	465	Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	1.91e-61	68	615	16	560	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	3.58e-60	109	615	61	560	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|M4DUF2|ASO_BRARP	6.60e-60	102	616	14	543	L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.76e-59	107	609	22	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|J9VQZ4|LAC2_CRYNH	2.02e-59	109	615	61	560	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999979	0.000042

TMHMM  Annotations     

Start	End
36	58